Solution NMR Backbone Assignment of the C-Terminal Region of Human Dynein Light Intermediate Chain 2 (LIC2-C) Unveils Structural Resemblance with Its Homologue LIC1-C

Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adaptor binding. In contrast to the vertebrate LIC hom...

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Vydáno v:Magnetochemistry Ročník 9; číslo 7; s. 166
Hlavní autoři: Henen, Morkos A., Paukovich, Natasia, Prekeris, Rytis, Vögeli, Beat
Médium: Journal Article
Jazyk:angličtina
Vydáno: Switzerland MDPI AG 01.07.2023
Témata:
Adapters
Analysis
Cell division
Chemical equilibrium
Dynein
Experiments
Helices
Homology
human dynein
Identification and classification
LIC2
light intermediate chain
NMR
Nuclear magnetic resonance
Phosphorylation
Properties
Protein expression
Proteins
Software
Spectrum analysis
SSP
Structure
Vertebrates
United States
SSP
human dynein
light intermediate chain
LIC2
ISSN:2312-7481, 2312-7481
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Abstract Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adaptor binding. In contrast to the vertebrate LIC homolog LIC1, LIC2 has received relatively limited characterization thus far, despite partially orthogonal functional roles. In this study, we present a near-to-complete backbone NMR chemical shift assignment of the C-terminal region of the light intermediate chain 2 of human dynein 1 (LIC2-C). We perform a comparative analysis of the secondary structure propensity of LIC2-C with the one previously reported for LIC1-C and show that the two transient helices in LIC1 that interact with motor adaptors are also present in LIC2.
AbstractList Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adaptor binding. In contrast to the vertebrate LIC homolog LIC1, LIC2 has received relatively limited characterization thus far, despite partially orthogonal functional roles. In this study, we present a near-to-complete backbone NMR chemical shift assignment of the C-terminal region of the light intermediate chain 2 of human dynein 1 (LIC2-C). We perform a comparative analysis of the secondary structure propensity of LIC2-C with the one previously reported for LIC1-C and show that the two transient helices in LIC1 that interact with motor adaptors are also present in LIC2.
Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adaptor binding. In contrast to the vertebrate LIC homolog LIC1, LIC2 has received relatively limited characterization thus far, despite partially orthogonal functional roles. In this study, we present a near-to-complete backbone NMR chemical shift assignment of the C-terminal region of the light intermediate chain 2 of human dynein 1 (LIC2-C). We perform a comparative analysis of the secondary structure propensity of LIC2-C with the one previously reported for LIC1-C and show that the two transient helices in LIC1 that interact with motor adaptors are also present in LIC2.Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adaptor binding. In contrast to the vertebrate LIC homolog LIC1, LIC2 has received relatively limited characterization thus far, despite partially orthogonal functional roles. In this study, we present a near-to-complete backbone NMR chemical shift assignment of the C-terminal region of the light intermediate chain 2 of human dynein 1 (LIC2-C). We perform a comparative analysis of the secondary structure propensity of LIC2-C with the one previously reported for LIC1-C and show that the two transient helices in LIC1 that interact with motor adaptors are also present in LIC2.
Audience Academic
Author Prekeris, Rytis
Paukovich, Natasia
Henen, Morkos A.
Vögeli, Beat
AuthorAffiliation 1 Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA
2 Department of Cell and Developmental Biology, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA
AuthorAffiliation_xml – name: 1 Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA
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CitedBy_id crossref_primary_10_1002_jcla_25030
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Keywords SSP
human dynein
light intermediate chain
LIC2
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Author Contributions: M.A.H., R.P. and B.V. conceptualized the project. M.A.H. and B.V. wrote the manuscript. M.A.H. and N.P. carried out experiments. M.A.H. analyzed data. B.V. and M.A.H. supervised the project and acquired funding. All authors have read and agreed to the published version of the manuscript.
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Snippet Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits,...
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SubjectTerms Adapters
Analysis
Cell division
Chemical equilibrium
Dynein
Experiments
Helices
Homology
human dynein
Identification and classification
LIC2
light intermediate chain
NMR
Nuclear magnetic resonance
Phosphorylation
Properties
Protein expression
Proteins
Software
Spectrum analysis
SSP
Structure
Vertebrates
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Title Solution NMR Backbone Assignment of the C-Terminal Region of Human Dynein Light Intermediate Chain 2 (LIC2-C) Unveils Structural Resemblance with Its Homologue LIC1-C
URI https://www.ncbi.nlm.nih.gov/pubmed/37476506
https://www.proquest.com/docview/2843078141
https://www.proquest.com/docview/2841023645
https://pubmed.ncbi.nlm.nih.gov/PMC10358425
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Volume 9
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