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PDBsum entry 5a4x
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Lipid binding protein
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PDB id
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5a4x
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References listed in PDB file
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Key reference
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Title
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Calcium-Dependent oligomerization of car proteins at cell membrane modulates aba signaling.
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Authors
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M.Diaz,
M.J.Sanchez-Barrena,
J.M.Gonzalez-Rubio,
L.Rodriguez,
D.Fernandez,
R.Antoni,
C.Yunta,
B.Belda-Palazon,
M.Gonzalez-Guzman,
M.Peirats-Llobet,
M.Menendez,
J.Boskovic,
J.A.Marquez,
P.L.Rodriguez,
A.Albert.
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Ref.
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Proc Natl Acad Sci U S A, 2016,
113,
E396.
[DOI no: ]
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PubMed id
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Abstract
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Regulation of ion transport in plants is essential for cell function. Abiotic
stress unbalances cell ion homeostasis, and plants tend to readjust it,
regulating membrane transporters and channels. The plant hormone abscisic acid
(ABA) and the second messenger Ca(2+) are central in such processes, as they are
involved in the regulation of protein kinases and phosphatases that control ion
transport activity in response to environmental stimuli. The identification and
characterization of the molecular mechanisms underlying the effect of ABA and
Ca(2+) signaling pathways on membrane function are central and could provide
opportunities for crop improvement. The C2-domain ABA-related (CAR) family of
small proteins is involved in the Ca(2+)-dependent recruitment of the pyrabactin
resistance 1/PYR1-like (PYR/PYL) ABA receptors to the membrane. However, to
fully understand CAR function, it is necessary to define a molecular mechanism
that integrates Ca(2+) sensing, membrane interaction, and the recognition of the
PYR/PYL interacting partners. We present structural and biochemical data showing
that CARs are peripheral membrane proteins that functionally cluster on the
membrane and generate strong positive membrane curvature in a Ca(2+)-dependent
manner. These features represent a mechanism for the generation, stabilization,
and/or specific recognition of membrane discontinuities. Such structures may act
as signaling platforms involved in the recruitment of PYR/PYL receptors and
other signaling components involved in cell responses to stress.
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