ArticleThe Journal of cell biology2017
Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis.
Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The Yeast Gsk-3 Kinase Mck1 Is Necessary for Cell Wall Remodeling in Glucose-Starved and Cell Wall-Stressed Cells.International journal of molecular sciences · 2025Article
- Review
- Bsp1, a fungal CPI motif protein, regulates actin filament capping in endocytosis and cytokinesis.Molecular biology of the cell · 2024Article
- Mechanism of actin capping protein recruitment and turnover during clathrin-mediated endocytosis.The Journal of cell biology · 2024Article
- Actin- and microtubule-based motors contribute to clathrin-independent endocytosis in yeast.Molecular biology of the cell · 2023Article
- Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate mitotic and male meiotic spindle bipolarity.Nature communications · 2023Article
- The dynein light chain protein Tda2 functions as a dimerization engine to regulate actin capping protein during endocytosis.Molecular biology of the cell · 2021Article
- Capping Protein Insulates Arp2/3-Assembled Actin Patches from Formins.Current biology : CB · 2019Article
- TheJournal of cell science · 2019Article
- Article
- The Sla1 adaptor-clathrin interaction regulates coat formation and progression of endocytosis.Traffic (Copenhagen, Denmark) · 2018Article
- Yeast Aim21/Tda2 both regulates free actin by reducing barbed end assembly and forms a complex with Cap1/Cap2 to balance actin assembly between patches and cables.Molecular biology of the cell · 2018Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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