Differential roles of two DDX17 isoforms in the formation of membraneless organelles

The RNA helicase, DDX17 is a member of the DEAD-box protein family. DDX17 has two isoforms: p72 and p82. The p82 isoform has additional amino acid sequences called intrinsically disordered regions (IDRs), which are related to the formation of membraneless organelles (MLOs). Here, we reveal that p72...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of biochemistry (Tokyo) Jg. 168; H. 1; S. 33
Hauptverfasser: Hirai, Yuya, Domae, Eisuke, Yoshikawa, Yoshihiro, Tomonaga, Keizo
Format: Journal Article
Sprache:Englisch
Veröffentlicht: England 01.07.2020
Schlagworte:
ISSN:1756-2651, 1756-2651
Online-Zugang:Weitere Angaben
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Abstract The RNA helicase, DDX17 is a member of the DEAD-box protein family. DDX17 has two isoforms: p72 and p82. The p82 isoform has additional amino acid sequences called intrinsically disordered regions (IDRs), which are related to the formation of membraneless organelles (MLOs). Here, we reveal that p72 is mostly localized to the nucleoplasm, while p82 is localized to the nucleoplasm and nucleoli. Additionally, p82 exhibited slower intranuclear mobility than p72. Furthermore, the enzymatic mutants of both p72 and p82 accumulate into the stress granules. The enzymatic mutant of p82 abolishes nucleolar localization of p82. Our findings suggest the importance of IDRs and enzymatic activity of DEAD-box proteins in the intracellular distribution and formation of MLOs.
AbstractList The RNA helicase, DDX17 is a member of the DEAD-box protein family. DDX17 has two isoforms: p72 and p82. The p82 isoform has additional amino acid sequences called intrinsically disordered regions (IDRs), which are related to the formation of membraneless organelles (MLOs). Here, we reveal that p72 is mostly localized to the nucleoplasm, while p82 is localized to the nucleoplasm and nucleoli. Additionally, p82 exhibited slower intranuclear mobility than p72. Furthermore, the enzymatic mutants of both p72 and p82 accumulate into the stress granules. The enzymatic mutant of p82 abolishes nucleolar localization of p82. Our findings suggest the importance of IDRs and enzymatic activity of DEAD-box proteins in the intracellular distribution and formation of MLOs.
The RNA helicase, DDX17 is a member of the DEAD-box protein family. DDX17 has two isoforms: p72 and p82. The p82 isoform has additional amino acid sequences called intrinsically disordered regions (IDRs), which are related to the formation of membraneless organelles (MLOs). Here, we reveal that p72 is mostly localized to the nucleoplasm, while p82 is localized to the nucleoplasm and nucleoli. Additionally, p82 exhibited slower intranuclear mobility than p72. Furthermore, the enzymatic mutants of both p72 and p82 accumulate into the stress granules. The enzymatic mutant of p82 abolishes nucleolar localization of p82. Our findings suggest the importance of IDRs and enzymatic activity of DEAD-box proteins in the intracellular distribution and formation of MLOs.The RNA helicase, DDX17 is a member of the DEAD-box protein family. DDX17 has two isoforms: p72 and p82. The p82 isoform has additional amino acid sequences called intrinsically disordered regions (IDRs), which are related to the formation of membraneless organelles (MLOs). Here, we reveal that p72 is mostly localized to the nucleoplasm, while p82 is localized to the nucleoplasm and nucleoli. Additionally, p82 exhibited slower intranuclear mobility than p72. Furthermore, the enzymatic mutants of both p72 and p82 accumulate into the stress granules. The enzymatic mutant of p82 abolishes nucleolar localization of p82. Our findings suggest the importance of IDRs and enzymatic activity of DEAD-box proteins in the intracellular distribution and formation of MLOs.
Author Yoshikawa, Yoshihiro
Hirai, Yuya
Tomonaga, Keizo
Domae, Eisuke
Author_xml – sequence: 1
  givenname: Yuya
  surname: Hirai
  fullname: Hirai, Yuya
  organization: Department of Biology, Osaka Dental University, 8-1, Kuzuha Hanazono-cho, Hirakata, Osaka 573-1121, Japan
– sequence: 2
  givenname: Eisuke
  surname: Domae
  fullname: Domae, Eisuke
  organization: Department of Biochemistry, Osaka Dental University, 8-1, Kuzuha Hanazono-cho, Hirakata, Osaka 573-1121, Japan
– sequence: 3
  givenname: Yoshihiro
  surname: Yoshikawa
  fullname: Yoshikawa, Yoshihiro
  organization: Department of Biochemistry, Osaka Dental University, 8-1, Kuzuha Hanazono-cho, Hirakata, Osaka 573-1121, Japan
– sequence: 4
  givenname: Keizo
  surname: Tomonaga
  fullname: Tomonaga, Keizo
  organization: Department of Virus Research, Institute for Frontier Life and Medical Sciences (InFRONT), Kyoto University, 53 Kawahara-cho, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32065632$$D View this record in MEDLINE/PubMed
BookMark eNpNkEtPwzAQhC1URB9w4QcgH7mE2uvYaY6o5SVV4lIkbpGdrCFVHRc7AfHvcUWROO030sxqdqdk1PkOCbnk7IazUsy3Zu4-tWYgTsiEF1JloCQf_eMxmca4ZQw4CHFGxgKYkkrAhGxWrbUYsOtbvaPB7zBSb2n_5elq9coL2kZvfXCRth3t35EehO5b3x1sDp0JusOUSrHwdsDE5-TU6l3Ei-OckZf7u83yMVs_Pzwtb9dZnYu8zxZcc-SYA9aCS2OVkiwJCcCKBdaNbUpp8qaphRFCgbG8tHlemqaQgiEDmJHr37374D8GjH3l2linCqmHH2IFQiq5KCFdOiNXR-tgHDbVPrROh-_q7xPwA1ILYVc
CitedBy_id crossref_primary_10_1172_JCI148130
crossref_primary_10_1016_j_tibs_2022_10_001
crossref_primary_10_1073_pnas_2022121118
crossref_primary_10_1007_s00401_021_02333_z
ContentType Journal Article
Copyright The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.
Copyright_xml – notice: The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.
DBID CGR
CUY
CVF
ECM
EIF
NPM
7X8
DOI 10.1093/jb/mvaa023
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList MEDLINE
MEDLINE - Academic
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: 7X8
  name: MEDLINE - Academic
  url: https://search.proquest.com/medline
  sourceTypes: Aggregation Database
DeliveryMethod no_fulltext_linktorsrc
Discipline Anatomy & Physiology
EISSN 1756-2651
ExternalDocumentID 32065632
Genre Journal Article
GroupedDBID ---
-E4
-~X
.2P
.CO
.I3
0R~
18M
29J
4.4
482
48X
53G
5GY
5RE
5WA
5WD
70D
A8Z
AAILS
AAIMJ
AAJKP
AAMDB
AAMVS
AAOGV
AAPQZ
AAPXW
AARHZ
AAUAY
AAUQX
AAVAP
AAVLN
ABDBF
ABDFA
ABEJV
ABEUO
ABGNP
ABIXL
ABJNI
ABMNT
ABNKS
ABPQP
ABPTD
ABQLI
ABVGC
ABWST
ABXVV
ABXZS
ABZBJ
ACGFO
ACGFS
ACIWK
ACNCT
ACPRK
ACUFI
ACUHS
ACUTJ
ADBBV
ADCFL
ADEYI
ADEZT
ADFTL
ADGKP
ADGZP
ADHKW
ADHZD
ADIPN
ADNBA
ADOCK
ADQBN
ADRTK
ADVEK
ADYVW
ADZTZ
ADZXQ
AEGPL
AEGXH
AEHKS
AEJOX
AEKSI
AELWJ
AEMDU
AENEX
AENZO
AEPUE
AETBJ
AEWNT
AFFZL
AFGWE
AFIYH
AFOFC
AFRAH
AFYAG
AGINJ
AGKEF
AGQXC
AGSYK
AHXPO
AIAGR
AIJHB
AJEEA
AJNCP
AKHUL
AKWXX
ALMA_UNASSIGNED_HOLDINGS
ALUQC
ALXQX
APIBT
APWMN
ARIXL
ATGXG
AXUDD
AYOIW
BAYMD
BCRHZ
BEYMZ
BHONS
BQDIO
BSWAC
C45
CDBKE
CGR
CS3
CUY
CVF
CZ4
DAKXR
DILTD
D~K
EBD
EBS
ECM
EE~
EIF
EMOBN
ESX
F5P
F9B
FHSFR
FLUFQ
FOEOM
FQBLK
GAUVT
GJXCC
H13
H5~
HAR
HW0
HZ~
IOX
J21
JSH
JXSIZ
KAQDR
KBUDW
KOP
KSI
KSN
L7B
M-Z
M49
N9A
NGC
NLBLG
NOMLY
NPM
NU-
O9-
OAWHX
OBOKY
ODMLO
OJQWA
OJZSN
OVD
OWPYF
P2P
PAFKI
PEELM
PQQKQ
Q1.
Q5Y
R44
RD5
ROL
ROX
ROZ
RUSNO
RW1
RXO
SV3
TEORI
TLC
TN5
TUS
TWZ
WH7
X7H
YAYTL
YKOAZ
YROCO
YXANX
ZKX
~91
~KM
7X8
AHGBF
AJBYB
ESTFP
ID FETCH-LOGICAL-c434t-81a1e1e42ec315bf665042e522078ecdfd95b4ddc3b3362bf19f449bd7530e022
IEDL.DBID 7X8
ISICitedReferencesCount 4
ISICitedReferencesURI http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000562477600005&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN 1756-2651
IngestDate Sun Sep 28 06:40:53 EDT 2025
Thu Apr 03 07:07:41 EDT 2025
IsPeerReviewed true
IsScholarly true
Issue 1
Keywords DDX17
nucleolus
stress granules
membraneless organelles
intrinsically disordered regions
Language English
License The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c434t-81a1e1e42ec315bf665042e522078ecdfd95b4ddc3b3362bf19f449bd7530e022
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 32065632
PQID 2356589263
PQPubID 23479
ParticipantIDs proquest_miscellaneous_2356589263
pubmed_primary_32065632
PublicationCentury 2000
PublicationDate 2020-07-01
PublicationDateYYYYMMDD 2020-07-01
PublicationDate_xml – month: 07
  year: 2020
  text: 2020-07-01
  day: 01
PublicationDecade 2020
PublicationPlace England
PublicationPlace_xml – name: England
PublicationTitle Journal of biochemistry (Tokyo)
PublicationTitleAlternate J Biochem
PublicationYear 2020
SSID ssj0021233
Score 2.3161678
Snippet The RNA helicase, DDX17 is a member of the DEAD-box protein family. DDX17 has two isoforms: p72 and p82. The p82 isoform has additional amino acid sequences...
SourceID proquest
pubmed
SourceType Aggregation Database
Index Database
StartPage 33
SubjectTerms Cell Nucleolus - metabolism
Cell Nucleus - metabolism
DEAD-box RNA Helicases - metabolism
Female
HeLa Cells
Humans
Organelles - metabolism
Protein Isoforms
RNA - metabolism
Uterine Cervical Neoplasms - metabolism
Uterine Cervical Neoplasms - pathology
Title Differential roles of two DDX17 isoforms in the formation of membraneless organelles
URI https://www.ncbi.nlm.nih.gov/pubmed/32065632
https://www.proquest.com/docview/2356589263
Volume 168
WOSCitedRecordID wos000562477600005&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText
inHoldings 1
isFullTextHit
isPrint
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LSwMxEA5qPXjxVR_1RQTxFrp57CMnKdbixdJDhb0tm2wCFbtb3Vrx3ztJt_UkCF4WFjYQspOZ75uZ5EPoRjGqbaxiYnmiiYCQSnJjFQkALIvEKsuZ9mIT8XCYpKkcNQm3ummrXPlE76iLSrsceZdxgB6JZBG_m70RpxrlqquNhMYmanGAMs6q43RdRXBe2TfYx2FEWBTS1fWkkndfVHe6yPPAyRT9Bi19iBns_Xdy-2i3AZe4t7SGA7RhykPU7pVArKdf-Bb7dk-fR2-jcb-RRoEt_opdk2GNK4vnnxXu91Ma40ldOUBb40mJASXi9TFH99nUTIFmlxCzahjmznO6AkB9hJ4HD-P7R9JILBAtuJiThObUUCOY0ZyGykYA2OAFQBlAB6MLW8hQiaLQXHEIdcpSaYWQqgCWExiI_8doq6xKc4pwEmobGg4EzEgR2FABOcppIq0JkiLiooOuV2uXgQm7ugTMrfqos5_V66CT5Q_IZsu7NjLOACNFnJ39YfQ52mGODftm2gvUsrCBzSXa1ov5pH6_8rYBz-Ho6Rvpm8T7
linkProvider ProQuest
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Differential+roles+of+two+DDX17+isoforms+in+the+formation+of+membraneless+organelles&rft.jtitle=Journal+of+biochemistry+%28Tokyo%29&rft.au=Hirai%2C+Yuya&rft.au=Domae%2C+Eisuke&rft.au=Yoshikawa%2C+Yoshihiro&rft.au=Tomonaga%2C+Keizo&rft.date=2020-07-01&rft.eissn=1756-2651&rft.volume=168&rft.issue=1&rft.spage=33&rft_id=info:doi/10.1093%2Fjb%2Fmvaa023&rft_id=info%3Apmid%2F32065632&rft_id=info%3Apmid%2F32065632&rft.externalDocID=32065632
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1756-2651&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1756-2651&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1756-2651&client=summon