The Sla1 adaptor-clathrin interaction regulates coat formation and progression of endocytosis.

Autor: Tolsma TO; Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado., Cuevas LM; Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado., Di Pietro SM; Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado.
Jazyk: angličtina
Zdroj: Traffic (Copenhagen, Denmark) [Traffic] 2018 Jun; Vol. 19 (6), pp. 446-462. Date of Electronic Publication: 2018 Apr 11.
DOI: 10.1111/tra.12563
Abstrakt: Clathrin-mediated endocytosis is a fundamental transport pathway that depends on numerous protein-protein interactions. Testing the importance of the adaptor protein-clathrin interaction for coat formation and progression of endocytosis in vivo has been difficult due to experimental constrains. Here, we addressed this question using the yeast clathrin adaptor Sla1, which is unique in showing a cargo endocytosis defect upon substitution of 3 amino acids in its clathrin-binding motif (sla1 AAA ) that disrupt clathrin binding. Live-cell imaging showed an impaired Sla1-clathrin interaction causes reduced clathrin levels but increased Sla1 levels at endocytic sites. Moreover, the rate of Sla1 recruitment was reduced indicating proper dynamics of both clathrin and Sla1 depend on their interaction. sla1 AAA cells showed a delay in progression through the various stages of endocytosis. The Arp2/3-dependent actin polymerization machinery was present for significantly longer time before actin polymerization ensued, revealing a link between coat formation and activation of actin polymerization. Ultimately, in sla1 AAA cells a larger than normal actin network was formed, dramatically higher levels of various machinery proteins other than clathrin were recruited, and the membrane profile of endocytic invaginations was longer. Thus, the Sla1-clathrin interaction is important for coat formation, regulation of endocytic progression and membrane bending.
(© 2018 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.)
Databáze: MEDLINE
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