6a9y | pdb_00006a9y
The crystal structure of Mu homology domain of SGIP1
Structural highlights
FunctionSGIP1_HUMAN May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis (By similarity). Publication Abstract from PubMedAlong with its homologs FCHo1 and FCHo2, SGIP1 plays an important role in clathrin-mediated endocytosis. The highly conserved C-terminal muHD domains in these proteins are the critical regions interacting with adapter molecules such as Eps15. The crystal structure of muHD domain of SGIP1 has been reported previously. In this study, we found that muHD domain of SGIP1 is capable of forming a stable dimer by an intermolecular disulfide bond formed by C632 in our crystal structure. The mutational study of C632 revealed that this residue is important for the function of SGIP1 during cellular endocytosis. Our study revealed a new dimerization and/or oligomerization manner in theses adaptor proteins, which is a critical prerequisite for their proper function. SGIP1 dimerizes via intermolecular disulfide bond in muHD domain during cellular endocytosis.,Zhang Y, Feng Y, Xin Y, Liu X Biochem Biophys Res Commun. 2018 Sep 18. pii: S0006-291X(18)32000-X. doi:, 10.1016/j.bbrc.2018.09.075. PMID:30236986[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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