Elucidation of Rab27 recruitment by its effectors: structure of Rab27a bound to Exophilin4/Slp2-a (Q24336538)

GOA release 2020-03-11

author

Soichi Wakatsuki

8

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author name string

Leonard M G Chavas

1

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Kentaro Ihara

2

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Masato Kawasaki

3

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Seiji Torii

4

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Tamami Uejima

5

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Ryuichi Kato

6

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Tetsuro Izumi

The mammalian Rab family of small GTPases: definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily.

7

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language of work or name

English

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publication date

8 October 2008

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published in

Structure

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volume

16

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page(s)

1468-77

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issue

10

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cites work

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Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome

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TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

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Rab27A-binding protein Slp2-a is required for peripheral melanosome distribution and elongated cell shape in melanocytes.

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Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.

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Rab27 and its effectors in secretory granule exocytosis: a novel docking machinery composed of a Rab27.effector complex

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Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice

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A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells

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Exophilin4/Slp2-a targets glucagon granules to the plasma membrane through unique Ca2+-inhibitory phospholipid-binding activity of the C2A domain

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MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes

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Versatile role of Rab27 in membrane trafficking: focus on the Rab27 effector families.

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