Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 2, Pages 121-130Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1043
Keywords
-
Funding
- NIGMS NIH HHS [GM62414-04] Funding Source: Medline
Ask authors/readers for more resources
Huntingtin-interacting protein-1 related (HIP1R) has a crucial protein-trafficking role, mediating associations between actin and clathrin-coated structures at the plasma membrane and trans-Golgi network. Here, we characterize the F-actin-binding region of HIP1R, termed the talin-HIP1/R/Sla2p actin-tethering C-terminal homology ( THATCH) domain. The 1.9-angstrom crystal structure of the human HIP1R THATCH core reveals a large sequence-conserved surface patch created primarily by residues from the third and fourth helices of a unique five-helix bundle. Point mutations of seven contiguous patch residues produced significant decreases in F-actin binding. We also show that THATCH domains have a conserved C-terminal latch capable of oligomerizing the core, thereby modulating F-actin engagement. Collectively, these results establish a framework for investigating the links between endocytosis and actin dynamics mediated by THATCH domain - containing proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available