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Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain.

Abstract：

:We demonstrate that the major in vivo targets of brefeldin A (BFA) in the secretory pathway of budding yeast are the three members of the Sec7 domain family of ARF exchange factors: Gea1p and Gea2p (functionally interchangeable) and Sec7p. Specific residues within the Sec7 domain are important for BFA inhibition of ARF exchange activity, since mutations in these residues of Gea1p (sensitive to BFA) and of ARNO (resistant to BFA) reverse the sensitivity of each to BFA in vivo and in vitro. We show that the target of BFA inhibition of ARF exchange activity is an ARF-GDP-Sec7 domain protein complex, and that BFA acts to stabilize this complex to a greater extent for a BFA-sensitive Sec7 domain than for a resistant one.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Peyroche A,Antonny B,Robineau S,Acker J,Cherfils J,Jackson CL

doi

10.1016/s1097-2765(00)80455-4

subject

Has Abstract

pub_date

1999-03-01 00:00:00

pages

275-85

issue

3

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(00)80455-4

journal_volume

3

pub_type

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