Kinesin-related Smy1 enhances the Rab-dependent association of myosin-V with secretory cargo.

ABSTRACT: The mechanisms by which molecular motors associate with specific cargo is a central problem in cell organization. The kinesin-like protein Smy1 of budding yeast was originally identified by the ability of elevated levels to suppress a conditional myosin-V mutation (myo2-66), but its function with Myo2 remained mysterious. Subsequently, Myo2 was found to provide an essential role in delivery of secretory vesicles for polarized growth and in the transport of mitochondria for segregation. By isolating and characterizing myo2 smy1 conditional mutants, we uncover the molecular function of Smy1 as a factor that enhances the association of Myo2 with its receptor, the Rab Sec4, on secretory vesicles. The tail of Smy1-which binds Myo2-its central dimerization domain, and its kinesin-like head domai

SUBMITTER: Lwin KM 

PROVIDER: S-EPMC4966985 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature