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PDBsum entry 6n8s
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Lipid binding protein
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PDB id
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6n8s
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References listed in PDB file
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Key reference
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Title
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Structural insights into the apkc regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2.
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Authors
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L.Almagor,
I.S.Ufimtsev,
A.Ayer,
J.Li,
W.I.Weis.
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Ref.
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Proc Natl Acad Sci U S A, 2019,
116,
10804-10812.
[DOI no: ]
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PubMed id
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Abstract
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Metazoan cell polarity is controlled by a set of highly conserved proteins.
Lethal giant larvae (Lgl) functions in apical-basal polarity through
phosphorylation-dependent interactions with several other proteins as well as
the plasma membrane. Phosphorylation of Lgl by atypical protein kinase C (aPKC),
a component of the partitioning-defective (Par) complex in epithelial cells,
excludes Lgl from the apical membrane, a crucial step in the establishment of
epithelial cell polarity. We present the crystal structures of human Lgl2 in
both its unphosphorylated and aPKC-phosphorylated states. Lgl2 adopts a double
β-propeller structure that is unchanged by aPKC phosphorylation of an
unstructured loop in its second β-propeller, ruling out models of
phosphorylation-dependent conformational change. We demonstrate that
phosphorylation controls the direct binding of purified Lgl2 to negative
phospholipids in vitro. We also show that a coil-helix transition of this region
that is promoted by phosphatidylinositol 4,5-bisphosphate (PIP2) is
also phosphorylation-dependent, implying a highly effective phosphorylative
switch for membrane association.
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