5VKY

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

5VKY の概要

• エントリーDOI: 10.2210/pdb5vky/pdb
• 分子名称: Topoisomerase I damage affected protein 2 (2 entities in total)
• 機能のキーワード: dynein light chain clathrin mediated endocytosis, protein binding
• 由来する生物種: Saccharomyces cerevisiae (strain JAY291) (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31150.85

構造登録者

McDonald, S.M.,Di Pietro, S.M.,Peersen, O.B. (登録日: 2017-04-24, 公開日: 2017-07-12, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)