5VKY

Yeast Tda2 (YER071C) - a dynein light chain family member that works independently of the dynein motor complex and microtubules.

Summary for 5VKY

• Entry DOI: 10.2210/pdb5vky/pdb
• Descriptor: Topoisomerase I damage affected protein 2 (2 entities in total)
• Functional Keywords: dynein light chain clathrin mediated endocytosis, protein binding
• Biological source: Saccharomyces cerevisiae (strain JAY291) (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 31150.85

Authors

McDonald, S.M.,Di Pietro, S.M.,Peersen, O.B. (deposition date: 2017-04-24, release date: 2017-07-12, Last modification date: 2024-03-13)

Primary citation

Farrell, K.B.,McDonald, S.,Lamb, A.K.,Worcester, C.,Peersen, O.B.,Di Pietro, S.M.
Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis.
J. Cell Biol., 216:2565-2580, 2017

PubMed Abstract: Clathrin- and actin-mediated endocytosis is essential in eukaryotic cells. In this study, we demonstrate that Tda2 is a novel protein of the endocytic machinery necessary for normal internalization of native cargo in yeast. Tda2 has not been classified in any protein family. Unexpectedly, solving the crystal structure of Tda2 revealed it belongs to the dynein light chain family. However, Tda2 works independently of the dynein motor complex and microtubules. Tda2 forms a tight complex with the polyproline motif-rich protein Aim21, which interacts physically with the SH3 domain of the Arp2/3 complex regulator Bbc1. The Tda2-Aim21 complex localizes to endocytic sites in a Bbc1- and filamentous actin-dependent manner. Importantly, the Tda2-Aim21 complex interacts directly with and facilitates the recruitment of actin-capping protein, revealing barbed-end filament capping at endocytic sites to be a regulated event. Thus, we have uncovered a new layer of regulation of the actin cytoskeleton by a member of a conserved protein family that has not been previously associated with a function in endocytosis.

PubMed: 28706108
DOI: 10.1083/jcb.201604123

Experimental method

X-RAY DIFFRACTION (2.3 Å)