Ontology highlight
ABSTRACT:
SUBMITTER: Krokhotin A
PROVIDER: S-EPMC6774862 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Krokhotin Andrey A Sarker Muzaddid M Sevilla Ernesto Alva EA Costantini Lindsey M LM Griffith Jack D JD Campbell Sharon L SL Dokholyan Nikolay V NV
Structure (London, England : 1993) 20190815 10
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 ...[more]