The diversity of Rab GTPases in Entamoeba histolytica

Rab proteins are ubiquitous small GTP-binding proteins that form a highly conserved family and regulate vesicular trafficking. Recent completion of the genome of the enteric protozoan parasite Entamoeba histolytica enabled us to identify an extremely large number (>90) of putative Rab genes. Mult...

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Veröffentlicht in:Experimental parasitology Jg. 110; H. 3; S. 244 - 252
Hauptverfasser: Saito-Nakano, Yumiko, Loftus, Brendan J., Hall, Neil, Nozaki, Tomoyoshi
Format: Journal Article
Sprache:Englisch
Veröffentlicht: San Diego, CA Elsevier Inc 01.07.2005
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ISSN:0014-4894, 1090-2449
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Abstract Rab proteins are ubiquitous small GTP-binding proteins that form a highly conserved family and regulate vesicular trafficking. Recent completion of the genome of the enteric protozoan parasite Entamoeba histolytica enabled us to identify an extremely large number (>90) of putative Rab genes. Multiple alignment and phylogenic analysis of amebic, human, and yeast Rab showed that only 22 amebic Rab proteins including EhRab1, EhRab2, EhRab5, EhRab7, EhRab8, EhRab11, and EhRab21 showed significant similarity to Rab from other organisms. The 69 remaining amebic Rab proteins showed only moderate similarity (<40% identity) to Rab proteins from other organisms. Approximately one-third of Rab proteins including Rab7, Rab11, and RabC form 15 subfamilies, which contain up to nine isoforms. Approximately 70% of amebic Rab genes contain single or multiple introns, and this proportion is significantly higher than that of common genes in this organism. Twenty-five Rabs possess an atypical carboxyl terminus such as CXXX, XCXX, XXCX, XXXC, and no cysteine. We propose annotation of amebic Rab genes and discuss biological significance of this extraordinary diversity of EhRab proteins in this organism.
AbstractList Rab proteins are ubiquitous small GTP-binding proteins that form a highly conserved family and regulate vesicular trafficking. Recent completion of the genome of the enteric protozoan parasite Entamoeba histolytica enabled us to identify an extremely large number (>90) of putative Rab genes. Multiple alignment and phylogenic analysis of amebic, human, and yeast Rab showed that only 22 amebic Rab proteins including EhRab1, EhRab2, EhRab5, EhRab7, EhRab8, EhRab11, and EhRab21 showed significant similarity to Rab from other organisms. The 69 remaining amebic Rab proteins showed only moderate similarity (<40% identity) to Rab proteins from other organisms. Approximately one-third of Rab proteins including Rab7, Rab11, and RabC form 15 subfamilies, which contain up to nine isoforms. Approximately 70% of amebic Rab genes contain single or multiple introns, and this proportion is significantly higher than that of common genes in this organism. Twenty-five Rabs possess an atypical carboxyl terminus such as CXXX, XCXX, XXCX, XXXC, and no cysteine. We propose annotation of amebic Rab genes and discuss biological significance of this extraordinary diversity of EhRab proteins in this organism.
Rab proteins are ubiquitous small GTP-binding proteins that form a highly conserved family and regulate vesicular trafficking. Recent completion of the genome of the enteric protozoan parasite Entamoeba histolytica enabled us to identify an extremely large number (>90) of putative Rab genes. Multiple alignment and phylogenic analysis of amebic, human, and yeast Rab showed that only 22 amebic Rab proteins including EhRab1, EhRab2, EhRab5, EhRab7, EhRab8, EhRab11, and EhRab21 showed significant similarity to Rab from other organisms. The 69 remaining amebic Rab proteins showed only moderate similarity (<40% identity) to Rab proteins from other organisms. Approximately one-third of Rab proteins including Rab7, Rab11, and RabC form 15 subfamilies, which contain up to nine isoforms. Approximately 70% of amebic Rab genes contain single or multiple introns, and this proportion is significantly higher than that of common genes in this organism. Twenty-five Rabs possess an atypical carboxyl terminus such as CXXX, XCXX, XXCX, XXXC, and no cysteine. We propose annotation of amebic Rab genes and discuss biological significance of this extraordinary diversity of EhRab proteins in this organism.Rab proteins are ubiquitous small GTP-binding proteins that form a highly conserved family and regulate vesicular trafficking. Recent completion of the genome of the enteric protozoan parasite Entamoeba histolytica enabled us to identify an extremely large number (>90) of putative Rab genes. Multiple alignment and phylogenic analysis of amebic, human, and yeast Rab showed that only 22 amebic Rab proteins including EhRab1, EhRab2, EhRab5, EhRab7, EhRab8, EhRab11, and EhRab21 showed significant similarity to Rab from other organisms. The 69 remaining amebic Rab proteins showed only moderate similarity (<40% identity) to Rab proteins from other organisms. Approximately one-third of Rab proteins including Rab7, Rab11, and RabC form 15 subfamilies, which contain up to nine isoforms. Approximately 70% of amebic Rab genes contain single or multiple introns, and this proportion is significantly higher than that of common genes in this organism. Twenty-five Rabs possess an atypical carboxyl terminus such as CXXX, XCXX, XXCX, XXXC, and no cysteine. We propose annotation of amebic Rab genes and discuss biological significance of this extraordinary diversity of EhRab proteins in this organism.
Rab proteins are ubiquitous small GTP-binding proteins that form a highly conserved family and regulate vesicular trafficking. Recent completion of the genome of the enteric protozoan parasite Entamoeba histolytica enabled us to identify an extremely large number (>90) of putative Rab genes. Multiple alignment and phylogenic analysis of amebic, human, and yeast Rab showed that only 22 amebic Rab proteins including EhRab1, EhRab2, EhRab5, EhRab7, EhRab8, EhRab11, and EhRab21 showed significant similarity to Rab from other organisms. The 69 remaining amebic Rab proteins showed only moderate similarity (<40% identity) to Rab proteins from other organisms. Approximately one-third of Rab proteins including Rab7, Rab11, and RabC form 15 subfamilies, which contain up to nine isoforms. Approximately 70% of amebic Rab genes contain single or multiple introns, and this proportion is significantly higher than that of common genes in this organism. Twenty-five Rabs possess an atypical carboxyl terminus such as CXXX, XCXX, XXCX, XXXC, and no cysteine. We propose annotation of amebic Rab genes and discuss biological significance of this extraordinary diversity of EhRab proteins in this organism.
Author Saito-Nakano, Yumiko
Nozaki, Tomoyoshi
Loftus, Brendan J.
Hall, Neil
Author_xml – sequence: 1
  givenname: Yumiko
  surname: Saito-Nakano
  fullname: Saito-Nakano, Yumiko
  organization: Department of Parasitology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan
– sequence: 2
  givenname: Brendan J.
  surname: Loftus
  fullname: Loftus, Brendan J.
  organization: The Institute for Genomic Research, Rockville, MD 20850, USA
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  givenname: Neil
  surname: Hall
  fullname: Hall, Neil
  organization: The Institute for Genomic Research, Rockville, MD 20850, USA
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  givenname: Tomoyoshi
  surname: Nozaki
  fullname: Nozaki, Tomoyoshi
  email: nozaki@med.gunma-u.ac.jp
  organization: Department of Parasitology, Gunma University Graduate School of Medicine, 3-39-22 Showa-machi, Maebashi, Gunma 371-8511, Japan
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Cites_doi 10.1016/0378-1119(96)00232-6
10.1128/EC.4.4.827-831.2005
10.1038/nature03291
10.1091/mbc.e03-10-0777
10.1093/nar/22.22.4673
10.1091/mbc.10.1.47
10.1038/348125a0
10.1016/S0955-0674(97)80025-7
10.1091/mbc.10.6.1837
10.1016/S0166-6851(01)00311-5
10.1006/jmbi.2001.5072
10.1006/jmbi.2000.4010
10.1016/S0166-6851(01)00318-8
10.1074/jbc.M311478200
10.1074/jbc.M203064200
10.1038/35052055
10.1074/jbc.M403987200
10.1186/gb-2001-2-5-reviews3007
10.1016/S1369-5274(02)00335-1
10.1016/S0166-6851(00)00216-4
10.1016/S1471-4914(01)02227-4
10.1152/physrev.2001.81.1.153
10.1016/S0166-6851(03)00115-4
10.1016/S0166-6851(99)00133-4
10.1242/jcs.113.2.183
10.1242/jcs.01560
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Issue 3
Keywords Membrane traffic
Rab GTPase
GTP
DNA
Entamoeba histolytica
Phylogeny
EhRab
Protozoa
Lobosea
Parasite
Phytogeny
Language English
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References Seabra, Mules, Hume (bib20) 2002; 8
Stenmark, H., Olkkonen, V.M., 2001. The Rab GTPase family. Genome Biology 2, REVIEWS3007.1-3007.7
Thompson, Higgins, Gibson (bib25) 1994; 22
Simpson, Griffiths, Wessling-Resnick, Fransen, Bennett, Jones (bib21) 2004; 117
Okada, M., Huston, C.D., Mann, B.J., Petri, W.A.J., Kita, K., Nozaki, T., 2005. Proteomic analysis of phagocytosis in the enteric protozoan parasite
Pereira-Leal, Seabra (bib13) 2001; 313
Pereira-Leal, Seabra (bib12) 2000; 301
Novick, Zerial (bib10) 1997; 9
Loftus, B., Anderson, I., Davies, R., Alismark, U.C.M., Samuelson, J., Amedeo, P., Roncaglia, P., Berriman, M., Hirt, R.P., Mann, B.J. Nozaki, T., Suh, B., Pop, M., Duchene, M., Ackers, J., Tannich, E., Leippe, M., Hofer, M., Bruchhaus, I., Willhoeft, U., Bhattacharya, A., Chillingworth, T., Churcher, C., Hance, Z., Harris, B., Harris, D., Jagels, K., Moule, S., Mungall, K., Ormond, D., Squares, R., Whitehead, S., Guillén, N. Gilchrist, C., Stroup, S.E., Bhattacharya, S., Lohia, A., Foster, P.G., Sicheritz-Ponten, T., Weber, C., Singh, U., Mukherjee, C., Petri, Jr., W.A., Clark, C.G., Embley, T.M., Barrell, B., Fraser, C.M., Hall, N., 2005. The genome of the protist parasite
Temesvari, Harris, Stanley, Cardelli (bib24) 1999; 103
Saito-Nakano, Nakazawa, Shigeta, Takeuchi, Nozaki (bib18) 2001; 116
McGugan, Temesvari (bib8) 2003; 129
Juarez, Sanchez-Lopez, Stock, Olvera, Ramos, Alagon (bib3) 2001; 116
Lohia, Samuelson (bib7) 1996; 173
Saito-Nakano, Yasuda, Nakada-Tsukui, Leippe, Nozaki (bib19) 2004; 279
Rodriguez, Garcia-Perez, Garcia-Rivera, Lopez-Reyes, Mendoza, Ortiz-Navarrete, Orozco (bib16) 2000; 108
Eukaryotic Cell, in press
Rodman, Wandinger-Ness (bib15) 2000; 113
WHO/PAHO/UNESCO. 1997. A consultation with experts on amebiasis. Epidemiological Bulletin 18, 13–14
Petri (bib14) 2002; 5
Bourne, Sanders, McCormick (bib1) 1990; 348
Mohrmann, Gerez, Oorschot, Klumperman, van der Sluijs (bib9) 2002; 277
Zerial, McBride (bib28) 2001; 2
Saitou, Nei (bib17) 1987; 4
Tisdale (bib26) 1999; 10
Nature 433, 865–868
Kumagai, Makioka, Takeuchi, Nozaki (bib5) 2004; 279
Takai, Sasaki, Matozaki (bib23) 2001; 81
Junutula, De Maziere, Peden, Ervin, Advani, van Dijk, Klumperman, Scheller (bib4) 2004; 15
Casanova, Wang, Kumar, Bhartur, Navarre, Woodrum, Altschuler, Ray, Goldenring (bib2) 1999; 10
Juarez (10.1016/j.exppara.2005.02.021_bib3) 2001; 116
Rodriguez (10.1016/j.exppara.2005.02.021_bib16) 2000; 108
Petri (10.1016/j.exppara.2005.02.021_bib14) 2002; 5
Zerial (10.1016/j.exppara.2005.02.021_bib28) 2001; 2
Kumagai (10.1016/j.exppara.2005.02.021_bib5) 2004; 279
10.1016/j.exppara.2005.02.021_bib6
McGugan (10.1016/j.exppara.2005.02.021_bib8) 2003; 129
Lohia (10.1016/j.exppara.2005.02.021_bib7) 1996; 173
Mohrmann (10.1016/j.exppara.2005.02.021_bib9) 2002; 277
Saito-Nakano (10.1016/j.exppara.2005.02.021_bib18) 2001; 116
Casanova (10.1016/j.exppara.2005.02.021_bib2) 1999; 10
Novick (10.1016/j.exppara.2005.02.021_bib10) 1997; 9
Takai (10.1016/j.exppara.2005.02.021_bib23) 2001; 81
10.1016/j.exppara.2005.02.021_bib27
10.1016/j.exppara.2005.02.021_bib22
Saitou (10.1016/j.exppara.2005.02.021_bib17) 1987; 4
Simpson (10.1016/j.exppara.2005.02.021_bib21) 2004; 117
Thompson (10.1016/j.exppara.2005.02.021_bib25) 1994; 22
Saito-Nakano (10.1016/j.exppara.2005.02.021_bib19) 2004; 279
Pereira-Leal (10.1016/j.exppara.2005.02.021_bib12) 2000; 301
Bourne (10.1016/j.exppara.2005.02.021_bib1) 1990; 348
Junutula (10.1016/j.exppara.2005.02.021_bib4) 2004; 15
Rodman (10.1016/j.exppara.2005.02.021_bib15) 2000; 113
Temesvari (10.1016/j.exppara.2005.02.021_bib24) 1999; 103
Seabra (10.1016/j.exppara.2005.02.021_bib20) 2002; 8
Pereira-Leal (10.1016/j.exppara.2005.02.021_bib13) 2001; 313
10.1016/j.exppara.2005.02.021_bib11
Tisdale (10.1016/j.exppara.2005.02.021_bib26) 1999; 10
References_xml – volume: 5
  start-page: 443
  year: 2002
  end-page: 447
  ident: bib14
  article-title: Pathogenesis of amebiasis
  publication-title: Current Opinion in Microbiology
– volume: 4
  start-page: 406
  year: 1987
  end-page: 425
  ident: bib17
  article-title: The neighbour-joining method: a new method to reconstruct phylogenetic trees
  publication-title: Molecular Biology of Evolution
– reference: Okada, M., Huston, C.D., Mann, B.J., Petri, W.A.J., Kita, K., Nozaki, T., 2005. Proteomic analysis of phagocytosis in the enteric protozoan parasite
– volume: 301
  start-page: 1077
  year: 2000
  end-page: 1087
  ident: bib12
  article-title: The mammalian Rab family of small GTPases: definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily
  publication-title: Journal of Molecular Biology
– volume: 103
  start-page: 225
  year: 1999
  end-page: 241
  ident: bib24
  article-title: Early and late endosomal compartments of
  publication-title: Molecular and Biochemical Parasitology
– volume: 129
  start-page: 137
  year: 2003
  end-page: 146
  ident: bib8
  article-title: Characterization of a Rab11-like GTPase,
  publication-title: Molecular and Biochemical Parasitology
– volume: 2
  start-page: 107
  year: 2001
  end-page: 117
  ident: bib28
  article-title: Rab proteins as membrane organizers
  publication-title: Nature Reviews Molecular Cell Biology
– volume: 277
  start-page: 32029
  year: 2002
  end-page: 32035
  ident: bib9
  article-title: Rab4 function in membrane recycling from early endosomes depends on a membrane to cytoplasm cycle
  publication-title: Journal of Biological Chemistry
– volume: 173
  start-page: 205
  year: 1996
  end-page: 208
  ident: bib7
  article-title: Heterogeneity of
  publication-title: Gene
– reference: . Eukaryotic Cell, in press
– volume: 116
  start-page: 219
  year: 2001
  end-page: 222
  ident: bib18
  article-title: Identification and characterization of genes encoding novel Rab proteins from
  publication-title: Molecular and Biochemical Parasitology
– volume: 279
  start-page: 49497
  year: 2004
  end-page: 49507
  ident: bib19
  article-title: Rab5-associated vacuoles play a unique role in phagocytosis of the enteric protozoan parasite
  publication-title: Journal of Biological Chemistry
– reference: . Nature 433, 865–868
– reference: Stenmark, H., Olkkonen, V.M., 2001. The Rab GTPase family. Genome Biology 2, REVIEWS3007.1-3007.7
– volume: 116
  start-page: 223
  year: 2001
  end-page: 228
  ident: bib3
  article-title: Characterization of the
  publication-title: Molecular and Biochemical Parasitology
– volume: 108
  start-page: 199
  year: 2000
  end-page: 206
  ident: bib16
  article-title: An
  publication-title: Molecular and Biochemical Parasitology
– volume: 9
  start-page: 496
  year: 1997
  end-page: 504
  ident: bib10
  article-title: The diversity of Rab proteins in vesicle transport
  publication-title: Current Opinion in Cell Biology
– volume: 8
  start-page: 23
  year: 2002
  end-page: 30
  ident: bib20
  article-title: Rab GTPases, intracellular traffic and disease
  publication-title: Trends in Molecular Medicine
– reference: WHO/PAHO/UNESCO. 1997. A consultation with experts on amebiasis. Epidemiological Bulletin 18, 13–14
– volume: 113
  start-page: 183
  year: 2000
  end-page: 192
  ident: bib15
  article-title: Rab GTPases coordinate endocytosis
  publication-title: Journal of Cell Science
– volume: 10
  start-page: 47
  year: 1999
  end-page: 61
  ident: bib2
  article-title: Association of Rab25 and Rab11a with the apical recycling system of polarized Madin–Darby canine kidney cells
  publication-title: Molecular Biology of the Cell
– volume: 313
  start-page: 889
  year: 2001
  end-page: 901
  ident: bib13
  article-title: Evolution of the Rab family of small GTP-binding proteins
  publication-title: Journal of Molecular Biology
– volume: 10
  start-page: 1837
  year: 1999
  end-page: 1849
  ident: bib26
  article-title: A Rab2 mutant with impaired GTPase activity stimulates vesicle formation from pre-Golgi intermediates
  publication-title: Molecular Biology of the Cell
– volume: 15
  start-page: 2218
  year: 2004
  end-page: 2229
  ident: bib4
  article-title: Rab14 is involved in membrane trafficking between the Golgi complex and endosomes
  publication-title: Molecular Biology of the Cell
– volume: 117
  start-page: 6297
  year: 2004
  end-page: 6311
  ident: bib21
  article-title: A role for the small GTPase Rab21 in the early endocytic pathway
  publication-title: Journal of Cell Science
– volume: 22
  start-page: 4673
  year: 1994
  end-page: 4680
  ident: bib25
  article-title: CLUSTAL W: improving the. sensitivity of progressive multiple sequence alignment through sequence weighting, positive-specific gap penalties and weight matrix choice
  publication-title: Nucleic Acids Research
– volume: 279
  start-page: 2316
  year: 2004
  end-page: 2323
  ident: bib5
  article-title: Molecular cloning and characterization of a protein farnesyltransferase from the enteric protozoan parasite
  publication-title: Journal of Biological Chemistry
– volume: 81
  start-page: 153
  year: 2001
  end-page: 208
  ident: bib23
  article-title: Small GTP-binding proteins
  publication-title: Physiological Reviews
– reference: Loftus, B., Anderson, I., Davies, R., Alismark, U.C.M., Samuelson, J., Amedeo, P., Roncaglia, P., Berriman, M., Hirt, R.P., Mann, B.J. Nozaki, T., Suh, B., Pop, M., Duchene, M., Ackers, J., Tannich, E., Leippe, M., Hofer, M., Bruchhaus, I., Willhoeft, U., Bhattacharya, A., Chillingworth, T., Churcher, C., Hance, Z., Harris, B., Harris, D., Jagels, K., Moule, S., Mungall, K., Ormond, D., Squares, R., Whitehead, S., Guillén, N. Gilchrist, C., Stroup, S.E., Bhattacharya, S., Lohia, A., Foster, P.G., Sicheritz-Ponten, T., Weber, C., Singh, U., Mukherjee, C., Petri, Jr., W.A., Clark, C.G., Embley, T.M., Barrell, B., Fraser, C.M., Hall, N., 2005. The genome of the protist parasite
– volume: 348
  start-page: 125
  year: 1990
  end-page: 132
  ident: bib1
  article-title: The GTPase superfamily: a conserved switch for diverse cell functions
  publication-title: Nature
– volume: 173
  start-page: 205
  year: 1996
  ident: 10.1016/j.exppara.2005.02.021_bib7
  article-title: Heterogeneity of Entamoeba histolytica rac genes encoding p21rac homologues
  publication-title: Gene
  doi: 10.1016/0378-1119(96)00232-6
– ident: 10.1016/j.exppara.2005.02.021_bib11
  doi: 10.1128/EC.4.4.827-831.2005
– ident: 10.1016/j.exppara.2005.02.021_bib6
  doi: 10.1038/nature03291
– volume: 15
  start-page: 2218
  year: 2004
  ident: 10.1016/j.exppara.2005.02.021_bib4
  article-title: Rab14 is involved in membrane trafficking between the Golgi complex and endosomes
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e03-10-0777
– volume: 22
  start-page: 4673
  year: 1994
  ident: 10.1016/j.exppara.2005.02.021_bib25
  article-title: CLUSTAL W: improving the. sensitivity of progressive multiple sequence alignment through sequence weighting, positive-specific gap penalties and weight matrix choice
  publication-title: Nucleic Acids Research
  doi: 10.1093/nar/22.22.4673
– ident: 10.1016/j.exppara.2005.02.021_bib27
– volume: 10
  start-page: 47
  year: 1999
  ident: 10.1016/j.exppara.2005.02.021_bib2
  article-title: Association of Rab25 and Rab11a with the apical recycling system of polarized Madin–Darby canine kidney cells
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.10.1.47
– volume: 348
  start-page: 125
  year: 1990
  ident: 10.1016/j.exppara.2005.02.021_bib1
  article-title: The GTPase superfamily: a conserved switch for diverse cell functions
  publication-title: Nature
  doi: 10.1038/348125a0
– volume: 9
  start-page: 496
  year: 1997
  ident: 10.1016/j.exppara.2005.02.021_bib10
  article-title: The diversity of Rab proteins in vesicle transport
  publication-title: Current Opinion in Cell Biology
  doi: 10.1016/S0955-0674(97)80025-7
– volume: 10
  start-page: 1837
  year: 1999
  ident: 10.1016/j.exppara.2005.02.021_bib26
  article-title: A Rab2 mutant with impaired GTPase activity stimulates vesicle formation from pre-Golgi intermediates
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.10.6.1837
– volume: 116
  start-page: 223
  year: 2001
  ident: 10.1016/j.exppara.2005.02.021_bib3
  article-title: Characterization of the EhRab8 gene, a marker of the late stages of the secretory pathway of Entamoeba histolytica
  publication-title: Molecular and Biochemical Parasitology
  doi: 10.1016/S0166-6851(01)00311-5
– volume: 313
  start-page: 889
  year: 2001
  ident: 10.1016/j.exppara.2005.02.021_bib13
  article-title: Evolution of the Rab family of small GTP-binding proteins
  publication-title: Journal of Molecular Biology
  doi: 10.1006/jmbi.2001.5072
– volume: 301
  start-page: 1077
  year: 2000
  ident: 10.1016/j.exppara.2005.02.021_bib12
  article-title: The mammalian Rab family of small GTPases: definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily
  publication-title: Journal of Molecular Biology
  doi: 10.1006/jmbi.2000.4010
– volume: 116
  start-page: 219
  year: 2001
  ident: 10.1016/j.exppara.2005.02.021_bib18
  article-title: Identification and characterization of genes encoding novel Rab proteins from Entamoeba histolytica
  publication-title: Molecular and Biochemical Parasitology
  doi: 10.1016/S0166-6851(01)00318-8
– volume: 279
  start-page: 2316
  year: 2004
  ident: 10.1016/j.exppara.2005.02.021_bib5
  article-title: Molecular cloning and characterization of a protein farnesyltransferase from the enteric protozoan parasite Entamoeba histolytica
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.M311478200
– volume: 277
  start-page: 32029
  year: 2002
  ident: 10.1016/j.exppara.2005.02.021_bib9
  article-title: Rab4 function in membrane recycling from early endosomes depends on a membrane to cytoplasm cycle
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.M203064200
– volume: 2
  start-page: 107
  year: 2001
  ident: 10.1016/j.exppara.2005.02.021_bib28
  article-title: Rab proteins as membrane organizers
  publication-title: Nature Reviews Molecular Cell Biology
  doi: 10.1038/35052055
– volume: 279
  start-page: 49497
  year: 2004
  ident: 10.1016/j.exppara.2005.02.021_bib19
  article-title: Rab5-associated vacuoles play a unique role in phagocytosis of the enteric protozoan parasite Entamoeba histolytica
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.M403987200
– ident: 10.1016/j.exppara.2005.02.021_bib22
  doi: 10.1186/gb-2001-2-5-reviews3007
– volume: 4
  start-page: 406
  year: 1987
  ident: 10.1016/j.exppara.2005.02.021_bib17
  article-title: The neighbour-joining method: a new method to reconstruct phylogenetic trees
  publication-title: Molecular Biology of Evolution
– volume: 5
  start-page: 443
  year: 2002
  ident: 10.1016/j.exppara.2005.02.021_bib14
  article-title: Pathogenesis of amebiasis
  publication-title: Current Opinion in Microbiology
  doi: 10.1016/S1369-5274(02)00335-1
– volume: 108
  start-page: 199
  year: 2000
  ident: 10.1016/j.exppara.2005.02.021_bib16
  article-title: An Entamoeba histolytica rab-like encoding gene and protein: function and cellular location
  publication-title: Molecular and Biochemical Parasitology
  doi: 10.1016/S0166-6851(00)00216-4
– volume: 8
  start-page: 23
  year: 2002
  ident: 10.1016/j.exppara.2005.02.021_bib20
  article-title: Rab GTPases, intracellular traffic and disease
  publication-title: Trends in Molecular Medicine
  doi: 10.1016/S1471-4914(01)02227-4
– volume: 81
  start-page: 153
  year: 2001
  ident: 10.1016/j.exppara.2005.02.021_bib23
  article-title: Small GTP-binding proteins
  publication-title: Physiological Reviews
  doi: 10.1152/physrev.2001.81.1.153
– volume: 129
  start-page: 137
  year: 2003
  ident: 10.1016/j.exppara.2005.02.021_bib8
  article-title: Characterization of a Rab11-like GTPase, EhRab11, of Entamoeba histolytica
  publication-title: Molecular and Biochemical Parasitology
  doi: 10.1016/S0166-6851(03)00115-4
– volume: 103
  start-page: 225
  year: 1999
  ident: 10.1016/j.exppara.2005.02.021_bib24
  article-title: Early and late endosomal compartments of Entamoeba histolytica are enriched in cysteine proteases, acid phosphatase and several Ras-related Rab GTPases
  publication-title: Molecular and Biochemical Parasitology
  doi: 10.1016/S0166-6851(99)00133-4
– volume: 113
  start-page: 183
  year: 2000
  ident: 10.1016/j.exppara.2005.02.021_bib15
  article-title: Rab GTPases coordinate endocytosis
  publication-title: Journal of Cell Science
  doi: 10.1242/jcs.113.2.183
– volume: 117
  start-page: 6297
  year: 2004
  ident: 10.1016/j.exppara.2005.02.021_bib21
  article-title: A role for the small GTPase Rab21 in the early endocytic pathway
  publication-title: Journal of Cell Science
  doi: 10.1242/jcs.01560
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Snippet Rab proteins are ubiquitous small GTP-binding proteins that form a highly conserved family and regulate vesicular trafficking. Recent completion of the genome...
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SubjectTerms Amino Acid Sequence
Animals
Base Sequence
Biological and medical sciences
deoxyribonucleic acid
DNA
EhRab
Entamoeba histolytica
Entamoeba histolytica - classification
Entamoeba histolytica - enzymology
Entamoeba histolytica - genetics
Entamoeba histolytica Rab
Fundamental and applied biological sciences. Psychology
Genetic Variation
GTP
guanosine 5′-triphosphate
Humans
Life cycle. Host-agent relationship. Pathogenesis
Membrane traffic
Molecular Sequence Data
Phylogeny
Protozoa
rab GTP-Binding Proteins - chemistry
rab GTP-Binding Proteins - classification
rab GTP-Binding Proteins - genetics
Rab GTPase
Sequence Alignment
Sequence Homology, Amino Acid
Title The diversity of Rab GTPases in Entamoeba histolytica
URI https://dx.doi.org/10.1016/j.exppara.2005.02.021
https://www.ncbi.nlm.nih.gov/pubmed/15955319
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https://www.proquest.com/docview/20934807
https://www.proquest.com/docview/67933565
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