Access and utilization of long chain fatty acyl-CoA by zDHHC protein acyltransferases.
Access and utilization of long chain fatty acyl-CoA by zDHHC protein acyltransferases.
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DOI：
10.1016/j.sbi.2022.102463
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发表时间：
2022-12
影响因子：
6.8
通讯作者：
Banerjee, Anirban
中科院分区：
文献类型：
--
作者：
Puthenveetil, Robbins;Gomez-Navarro, Natalia;Banerjee, Anirban
S-acylation is a reversible posttranslational modification, where a long chain fatty acid is attached to a protein through a thioester linkage. Being the most abundant form of lipidation in humans, a family of twenty-three human zDHHC integral membrane enzymes catalyze this reaction. Previous structures of the apo and lipid bound zDHHCs shed light into the molecular details of the active site and binding pocket. Here we delve further into the details of fatty acyl-CoA recognition by zDHHC acyltransferases using molecular features from the recent structure. We additionally review indirect evidence that suggests acyl-CoAs do not diffuse freely in the cytosol, but are channeled into specific pathways, and comment on the suggested mechanisms for fatty acyl-CoA compartmentalization and intracellular transport, to finally speculate about the potential mechanisms that underlie fatty acyl-CoA delivery to zDHHC enzymes.
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DOI：
10.1073/pnas.2022050119
发表时间：
2022-02-15
影响因子：
11.1
作者：
Lee CJ;Stix R;Rana MS;Shikwana F;Murphy RE;Ghirlando R;Faraldo-Gómez JD;Banerjee A
通讯作者：
Banerjee A
影响因子：
16
作者：
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通讯作者：
Siebold C
DOI：
10.1007/978-1-4939-9532-5_16
发表时间：
2019-01-01
期刊：
PROTEIN LIPIDATION: METHODS AND PROTOCOLS
影响因子：
--
作者：
Blanc, Mathieu;David, Fabrice P. A.;van der Goot, F. Gisou
通讯作者：
van der Goot, F. Gisou
影响因子：
3.3
作者：
Joyce, CW;Shelness, GS;Rudel, LL
通讯作者：
Rudel, LL
影响因子：
8.1
作者：
Bowman TA;O'Keeffe KR;D'Aquila T;Yan QW;Griffin JD;Killion EA;Salter DM;Mashek DG;Buhman KK;Greenberg AS
通讯作者：
Greenberg AS