Open AccessAdaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly
Author(s) -
Cameron Dale MacQuarrie,
MariaSanta C. Mangione,
Robert T. Carroll,
Michael L. James,
Kathleen L. Gould,
Vladimir Sirotkin
Publication year - 2019
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.233502
Subject(s) - endocytic cycle , endocytosis , microbiology and biotechnology , biology , actin , schizosaccharomyces , schizosaccharomyces pombe , saccharomyces cerevisiae , yeast , cell , biochemistry
Arp2/3 complex-nucleated branched actin networks provide key force necessary for endocytosis. The Arp2/3 complex is activated by Nucleation Promoting Factors including the Schizosaccharomyces pombe proteins WASp Wsp1 and myosin-1 Myo1. There are >40 known yeast endocytic proteins with distinct spatial and temporal localizations and functions; however, it is still unclear how these proteins work together to drive endocytosis. We used quantitative live cell imaging to determine the function of the uncharacterized S. pombe protein Bbc1. We discovered Myo1 interacts with and recruits Bbc1 to sites of endocytosis. Bbc1 competes with verprolin Vrp1 for localization to patches and association with Myo1, thus releasing Vrp1 and its binding partner Wsp1 from Myo1. Normally Myo1 remains at the base of the endocytic invagination and Vrp1-Wsp1 internalize with the endocytic vesicle. However, in the absence of Bbc1, a portion of Vrp1-Wsp1 remains with Myo1 at the base of the invagination and endocytic structures internalize twice as far. We propose that Bbc1 disrupts a transient interaction of Myo1 with Vrp1 and Wsp1 and thereby limits Arp2/3 complex-nucleation of actin branches at the plasma membrane.