Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3.
Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3.
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DOI:
10.1083/jcb.200602049
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发表时间:
2006-07-03
期刊:
影响因子:
--
通讯作者:
Conibear E
中科院分区:
文献类型:
--
作者:
Lam KK;Davey M;Sun B;Roth AF;Davis NG;Conibear E
The yeast chitin synthase Chs3 provides a well-studied paradigm for polytopic membrane protein trafficking. In this study, high-throughput analysis of the yeast deletion collection identifies a requirement for Pfa4, which is an uncharacterized protein with protein acyl transferase (PAT) homology, in Chs3 transport. PATs, which are the enzymatic mediators of protein palmitoylation, have only recently been discovered, and few substrates have been identified. We find that Chs3 is palmitoylated and that this modification is Pfa4-dependent, indicating that Pfa4 is indeed a PAT. Chs3 palmitoylation is required for ER export, but not for interaction with its dedicated ER chaperone, Chs7. Nonetheless, both palmitoylation and chaperone association are required to prevent the accumulation of Chs3 in high–molecular mass aggregates at the ER. Our data indicate that palmitoylation is necessary for Chs3 to attain an export-competent conformation, and suggest the possibility of a more general role for palmitoylation in the ER quality control of polytopic membrane proteins.
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影响因子:
7.8
作者:
Trilla, J A;Duran, A;Roncero, C
通讯作者:
Roncero, C
DOI:
10.1046/j.1432-1327.1998.2560419.x
发表时间:
1998-09-01
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
作者:
Cos, T;Ford, RA;Roncero, C
通讯作者:
Roncero, C
影响因子:
4.8
作者:
Lobo, S;Greentree, WK;Deschenes, RJ
通讯作者:
Deschenes, RJ
影响因子:
3.3
作者:
Malkus, P;Graham, LA;Schekman, R
通讯作者:
Schekman, R
DOI:
10.1073/pnas.1834246100
发表时间:
2003-09-02
影响因子:
11.1
作者:
Valdivia, RH;Schekman, R
通讯作者:
Schekman, R