4.4 Article Proceedings Paper

The Sla2p/HIP1/HIP1R family: similar structure, similar function in endocytosis?

Journal

BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 38, Issue -, Pages 187-191

Publisher

PORTLAND PRESS LTD
DOI: 10.1042/BST0380187

Keywords

AP180 N-terminal homology (ANTH); endocytosis; huntingtin-interacting protein 1 (HIP1); HIP1-related (HIP1R); Sla2p; talin-like domain

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HIP1 (huntingtin interacting protein 1) has two close relatives: HIP1R (HIP1-related) and yeast Sla2p. All three members of the family have a conserved domain structure, suggesting a common function. Over the past decade, a number of studies have characterized these proteins using a combination of biochemical, imaging, structural and genetic techniques. These studies provide valuable information on binding partners, structure and dynamics of HIP1/HIP1R/Sla2p. in general, all suggest a role in CME (clathrin-mediated endocytosis) for the three proteins, though some differences have emerged. In this mini-review we summarize the current views on the roles of these proteins, while emphasizing the unique attributes of each family member.

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