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PDBsum entry 4xoi
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References listed in PDB file
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Key reference
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Title
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Mechanistic insights into the anchorage of the contractile ring by anillin and mid1.
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Authors
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L.Sun,
R.Guan,
I.J.Lee,
Y.Liu,
M.Chen,
J.Wang,
J.Q.Wu,
Z.Chen.
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Ref.
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Dev Cell, 2015,
33,
413-426.
[DOI no: ]
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PubMed id
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Abstract
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Anillins and Mid1 are scaffold proteins that play key roles in anchorage of the
contractile ring at the cell equator during cytokinesis in animals and fungi,
respectively. Here, we report crystal structures and functional analysis of
human anillin and S. pombe Mid1. The combined data show anillin contains
a cryptic C2 domain and a Rho-binding domain. Together with the tethering PH
domain, three membrane-associating elements synergistically bind to RhoA and
phospholipids to anchor anillin at the cleavage furrow. Surprisingly, Mid1 also
binds to the membrane through a cryptic C2 domain. Dimerization of Mid1 leads to
high affinity and preference for PI(4,5)P2, which stably anchors Mid1 at the
division plane, bypassing the requirement for Rho GTPase. These findings uncover
the unexpected general machinery and the divergent regulatory logics for the
anchorage of the contractile ring through the anillin/Mid1 family proteins from
yeast to humans.
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