Reference - PMID:19808887 - Ste20-kinase-dependent TEDS-site phosphorylation modulates the dynamic localisation and endocytic function of the fission yeast class I myosin, Myo1.

Reference summary

PubMed ID

PMID:19808887

Title

Ste20-kinase-dependent TEDS-site phosphorylation modulates the dynamic localisation and endocytic function of the fission yeast class I myosin, Myo1.

Authors

Attanapola SL, Alexander CJ, Mulvihill DP

Citation

J Cell Sci 2009 Nov 01;122(Pt 21):3856-61

Publication year

2009

Abstract

Type I myosins are monomeric motors involved in a range of motile and sensory activities in different cell types. In simple unicellular eukaryotes, motor activity of class I myosins is regulated by phosphorylation of a conserved 'TEDS site' residue within the motor domain. The mechanism by which this phosphorylation event affects the cellular function of each myosin I remains unclear. The fission yeast myosin I, Myo1, activates Arp2/3-dependent polymerisation of cortical actin patches and also regulates endocytosis. Using mutants and Myo1-specific antibodies, we show that the phosphorylation of the Myo1 TEDS site (serine 361) plays a crucial role in regulating this protein's dynamic localisation and cellular function. We conclude that although phosphorylation of serine 361 does not affect the ability of this motor protein to promote actin polymerisation, it is required for Myo1 to recruit to sites of endocytosis and function during this process.

Annotation