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PDBsum entry 2kig
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Endocytosis, hydrolase
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PDB id
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2kig
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References listed in PDB file
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Key reference
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Title
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A ph domain within ocrl bridges clathrin-Mediated membrane trafficking to phosphoinositide metabolism.
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Authors
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Y.Mao,
D.M.Balkin,
R.Zoncu,
K.S.Erdmann,
L.Tomasini,
F.Hu,
M.M.Jin,
M.E.Hodsdon,
P.De camilli.
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Ref.
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Embo J, 2009,
28,
1831-1842.
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PubMed id
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Abstract
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OCRL, whose mutations are responsible for Lowe syndrome and Dent disease, and
INPP5B are two similar proteins comprising a central inositol 5-phosphatase
domain followed by an ASH and a RhoGAP-like domain. Their divergent NH2-terminal
portions remain uncharacterized. We show that the NH2-terminal region of OCRL,
but not of INPP5B, binds clathrin heavy chain. OCRL, which in contrast to INPP5B
visits late stage endocytic clathrin-coated pits, was earlier shown to contain
another binding site for clathrin in its COOH-terminal region. NMR structure
determination further reveals that despite their primary sequence dissimilarity,
the NH2-terminal portions of both OCRL and INPP5B contain a PH domain. The novel
clathrin-binding site in OCRL maps to an unusual clathrin-box motif located in a
loop of the PH domain, whose mutations reduce recruitment efficiency of OCRL to
coated pits. These findings suggest an evolutionary pressure for a specialized
function of OCRL in bridging phosphoinositide metabolism to clathrin-dependent
membrane trafficking.
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