Distinct Binding Modes of Vinculin Isoforms Underlie Their Functional Differences.

Actins Alternative Splicing Animals Binding Sites Cryoelectron Microscopy Models, Molecular Mutation Protein Binding Protein Domains Protein Structure, Secondary Vinculin / chemistry
actin cardiomyopathy heart metavinculin molecular dynamics vinculin

Journal

Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697

Informations de publication

Date de publication:
01 10 2019
Historique:
received: 16 03 2019
revised: 23 05 2019
accepted: 23 07 2019
pubmed: 20 8 2019
medline: 21 5 2020
entrez: 20 8 2019
Statut: ppublish

Résumé

Vinculin and its splice isoform metavinculin play key roles in regulating cellular morphology, motility, and force transduction. Vinculin is distinct from metavinculin in its ability to bundle filamentous actin (F-actin). To elucidate the molecular basis for these differences, we employed computational and experimental approaches. Results from these analyses suggest that the C terminus of both vinculin and metavinculin form stable interactions with the F-actin surface. However, the metavinculin tail (MVt) domain contains a 68 amino acid insert, with helix 1 (H1) sequestered into a globular subdomain, which protrudes from the F-actin surface and prevents actin bundling by sterically occluding actin filaments. Consistent with our model, deletion and selective point mutations within the MVt H1 disrupt this protruding structure, and facilitate actin bundling similar to vinculin tail (Vt) domain.

Identifiants

DOI: 10.1016/j.str.2019.07.013 PMID: 31422909 PMC: PMC6774862
pubmed: 31422909
pii: S0969-2126(19)30245-X
doi: 10.1016/j.str.2019.07.013
pmc: PMC6774862
mid: NIHMS1536233
pii:
doi:

Substances chimiques

Actins 0
metavinculin 0
Vinculin 125361-02-6

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

1527-1536.e3

Subventions

Organisme : NCI NIH HHS
ID : P01 CA019014
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM115597
Pays : United States
Organisme : NIGMS NIH HHS
ID : R25 GM060655
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM134962
Pays : United States

Informations de copyright

Copyright © 2019 Elsevier Ltd. All rights reserved.

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Auteurs

Andrey Krokhotin (A)

Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Departments of Pathology, Genetics and Developmental Biology, Howard Hughes Medical Institute, Stanford Medical School, Palo Alto, CA 94305, USA.

Muzaddid Sarker (M)

Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.

Ernesto Alva Sevilla (EA)

Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Lindsey M Costantini (LM)

Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Jack D Griffith (JD)

Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Sharon L Campbell (SL)

Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. Electronic address: campbesl@med.unc.edu.

Nikolay V Dokholyan (NV)

Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Departments of Pharmacology and Departments of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA 17033, USA. Electronic address: dokh@psu.edu.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Protéines des microfilaments › Actines › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Maturation post-transcriptionnelle des ARN › Épissage des ARN › Épissage alternatif › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Eucaryotes › Animaux › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Sites de fixation › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Techniques d'investigation › Microscopie électronique › Cryomicroscopie électronique › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Phénomènes génétiques › Variation génétique › Mutation › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Métabolisme › Liaison aux protéines › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure secondaire des protéines › Distinct Binding Modes of Vinculin Isoforms...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Vinculine › Distinct Binding Modes of Vinculin Isoforms...