Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases (Q27638775)

5

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Alexey Rak

2

object named as

Alexey Rak

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author name string

Alexandru-Tudor Constantinescu

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Heike Esters

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Axel J Scheidig

The GTPase superfamily: a conserved switch for diverse cell functions

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publication date

April 2002

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published in

Structure

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volume

10

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issue

4

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page(s)

569-79

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cites work

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Distinct structural elements of rab5 define its functional specificity.

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Specificity domains distinguish the Ras-related GTPases Ypt1 and Sec4.

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

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Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A

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The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance.

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New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion

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The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein

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Rab7: crystallization of intact and C-terminal truncated constructs complexed with GDP and GppNHp

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Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport

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Vps9, Rabex-5 and DSS4: proteins with weak but distinct nucleotide-exchange activities for Rab proteins

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