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Journal article

Biophysical analysis of the interaction of Rab6a GTPase with its effector domains.

Abstract:

Rab GTPases are key regulators of intracellular vesicular transport that control vesicle budding, cargo sorting, transport, tethering, and fusion. In the inactive (GDP-bound) conformation, Rab GTPases are targeted to intracellular compartments where they are converted into the active GTP-bound form and recruit effector domain containing proteins. Rab6a has been implicated in dynein-mediated vesicle movement at the Golgi apparatus and shown to interact with a plethora of effector proteins. In ...

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Publisher copy:
10.1074/jbc.m806003200

Authors


Bergbrede, T More by this author
Schoebel, S More by this author
Blankenfeldt, W More by this author
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Journal:
The Journal of biological chemistry
Volume:
284
Issue:
5
Pages:
2628-2635
Publication date:
2009-01-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:8a6b586f-3215-4b1e-b369-dad06a00caf9
Source identifiers:
310266
Local pid:
pubs:310266

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