Unknown

Dataset Information

0

Calmodulin Promotes N-BAR Domain-Mediated Membrane Constriction and Endocytosis.


ABSTRACT: Membrane remodeling by BAR (Bin, Amphiphysin, RVS) domain-containing proteins, such as endophilins and amphiphysins, is integral to the process of endocytosis. However, little is known about the regulation of endocytic BAR domain activity. We have identified an interaction between the yeast Rvs167 N-BAR domain and calmodulin. Calmodulin-binding mutants of Rvs167 exhibited defects in endocytic vesicle release. In vitro, calmodulin enhanced membrane tubulation and constriction by wild-type Rvs167 but not calmodulin-binding-defective mutants. A subset of mammalian N-BAR domains bound calmodulin, and co-expression of calmodulin with endophilin A2 potentiated tubulation in vivo. These studies reveal a conserved role for calmodulin in regulating the intrinsic membrane-sculpting activity of endocytic N-BAR domains.

SUBMITTER: Myers MD 

PROVIDER: S-EPMC4855880 | BioStudies | 2016-01-01

REPOSITORIES: biostudies

Similar Datasets

2016-01-01 | S-EPMC4982929 | BioStudies
2012-01-01 | S-EPMC3281743 | BioStudies
2006-01-01 | S-EPMC1500852 | BioStudies
2020-01-01 | S-EPMC7062783 | BioStudies
1000-01-01 | S-EPMC3328703 | BioStudies
2019-01-01 | S-EPMC6396150 | BioStudies
2015-01-01 | S-EPMC4328750 | BioStudies
1969-12-31 | S-SCDT-EMBOJ-2018-100116 | BioStudies
1000-01-01 | S-EPMC4311921 | BioStudies
2014-01-01 | S-EPMC4024918 | BioStudies