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Palmitoylation

About: Palmitoylation is a research topic. Over the lifetime, 2302 publications have been published within this topic receiving 126717 citations.


Papers
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Journal ArticleDOI
30 Jun 1989-Cell
TL;DR: It is shown that all ras proteins are polyisoprenylated on their C-terminal cysteine (Cys186) and palmitoylation increases the avidity of this binding and enhances their transforming activity.

1,750 citations

Journal ArticleDOI
TL;DR: The role of myristate and palmitate in promoting membrane binding as well as specific membrane targeting will be reviewed, with emphasis on the Src family of tyrosine protein kinases and alpha subunits of heterotrimeric G proteins.

1,271 citations

Journal ArticleDOI
05 Oct 1990-Cell
TL;DR: Within the hypervariable domain of p21K-ras(B), which is not palmitoylated, a novel plasma membrane targeting signal consisting of a polybasic domain that also acts in combination with the CAAX motif is identified.

1,064 citations

Journal ArticleDOI
TL;DR: Recent studies that have provided insights into the mechanisms that mediate the functional consequences of palmitate are reviewed.
Abstract: Palmitate modifies both peripheral and integral membrane proteins and its addition can be permanent or transient, which makes it unique among the lipid modifications of proteins. The presence of palmitate on a protein affects how the protein interacts with lipids and proteins in a membrane compartment, and the reversibility of palmitoylation allows different modes of trafficking between membrane compartments. Here, we review recent studies that have provided insights into the mechanisms that mediate the functional consequences of this versatile modification.

930 citations

Journal ArticleDOI
01 Aug 1998-Immunity
TL;DR: It is demonstrated that human LAT is palmitoylated and that palMIToylated LAT predominantly localizes into glycolipid-enriched microdomains (GEMs).

857 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023105
2022170
2021123
2020116
2019113
201888