Protein fatty acylation

A novel mechanism for association of proteins with membranes and its role in transmembrane regulatory pathways

J. S. Hu, G. James, E. N. Olson

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

A wide range of proteins of cellular and viral origin have been shown to be modified covalently by long-chain fatty acids. Recent studies have revealed at least two distinct types of protein fatty acylation which involve different fatty acyltransferases. The abundant fatty acid, palmitate, is incorporated post-translationally through a thiol ester linkage into a variety of cell surface glycoproteins and non-glycosylated intracellular proteins. In contrast, the rare fatty acid, myristate, is incorporated co-translationally through an amide linkage into numerous intracellular proteins. Identification of proteins that contain covalent fatty acids has revealed that this modification is common to a broad array of proteins that play important roles in transmembrane regulatory pathways. For many of these proteins, the fatty acid moiety appears to play an important role in directing the polypeptide to the appropriate membrane and in mediating protein-protein interactions within the membrane. This review will summarize recent studies that define different pathways for protein fatty acylation and will consider the potential functions for this unique covalent modification of proteins.

Original languageEnglish (US)
Pages (from-to)219-226
Number of pages8
JournalBioFactors
Volume1
Issue number3
StatePublished - 1988

Fingerprint

Acylation
Membrane Proteins
Association reactions
Membranes
Fatty Acids
Proteins
Acyltransferases
Protein Array Analysis
Palmitates
Membrane Glycoproteins
Myristic Acid
Viral Proteins
Sulfhydryl Compounds
Amides
Esters
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Protein fatty acylation : A novel mechanism for association of proteins with membranes and its role in transmembrane regulatory pathways. / Hu, J. S.; James, G.; Olson, E. N.

In: BioFactors, Vol. 1, No. 3, 1988, p. 219-226.

Research output: Contribution to journalArticle

@article{c062f3acc6364369bab93703a22356e0,
title = "Protein fatty acylation: A novel mechanism for association of proteins with membranes and its role in transmembrane regulatory pathways",
abstract = "A wide range of proteins of cellular and viral origin have been shown to be modified covalently by long-chain fatty acids. Recent studies have revealed at least two distinct types of protein fatty acylation which involve different fatty acyltransferases. The abundant fatty acid, palmitate, is incorporated post-translationally through a thiol ester linkage into a variety of cell surface glycoproteins and non-glycosylated intracellular proteins. In contrast, the rare fatty acid, myristate, is incorporated co-translationally through an amide linkage into numerous intracellular proteins. Identification of proteins that contain covalent fatty acids has revealed that this modification is common to a broad array of proteins that play important roles in transmembrane regulatory pathways. For many of these proteins, the fatty acid moiety appears to play an important role in directing the polypeptide to the appropriate membrane and in mediating protein-protein interactions within the membrane. This review will summarize recent studies that define different pathways for protein fatty acylation and will consider the potential functions for this unique covalent modification of proteins.",
author = "Hu, {J. S.} and G. James and Olson, {E. N.}",
year = "1988",
language = "English (US)",
volume = "1",
pages = "219--226",
journal = "BioFactors",
issn = "0951-6433",
publisher = "Wiley-Blackwell",
number = "3",

}

TY - JOUR

T1 - Protein fatty acylation

T2 - A novel mechanism for association of proteins with membranes and its role in transmembrane regulatory pathways

AU - Hu, J. S.

AU - James, G.

AU - Olson, E. N.

PY - 1988

Y1 - 1988

N2 - A wide range of proteins of cellular and viral origin have been shown to be modified covalently by long-chain fatty acids. Recent studies have revealed at least two distinct types of protein fatty acylation which involve different fatty acyltransferases. The abundant fatty acid, palmitate, is incorporated post-translationally through a thiol ester linkage into a variety of cell surface glycoproteins and non-glycosylated intracellular proteins. In contrast, the rare fatty acid, myristate, is incorporated co-translationally through an amide linkage into numerous intracellular proteins. Identification of proteins that contain covalent fatty acids has revealed that this modification is common to a broad array of proteins that play important roles in transmembrane regulatory pathways. For many of these proteins, the fatty acid moiety appears to play an important role in directing the polypeptide to the appropriate membrane and in mediating protein-protein interactions within the membrane. This review will summarize recent studies that define different pathways for protein fatty acylation and will consider the potential functions for this unique covalent modification of proteins.

AB - A wide range of proteins of cellular and viral origin have been shown to be modified covalently by long-chain fatty acids. Recent studies have revealed at least two distinct types of protein fatty acylation which involve different fatty acyltransferases. The abundant fatty acid, palmitate, is incorporated post-translationally through a thiol ester linkage into a variety of cell surface glycoproteins and non-glycosylated intracellular proteins. In contrast, the rare fatty acid, myristate, is incorporated co-translationally through an amide linkage into numerous intracellular proteins. Identification of proteins that contain covalent fatty acids has revealed that this modification is common to a broad array of proteins that play important roles in transmembrane regulatory pathways. For many of these proteins, the fatty acid moiety appears to play an important role in directing the polypeptide to the appropriate membrane and in mediating protein-protein interactions within the membrane. This review will summarize recent studies that define different pathways for protein fatty acylation and will consider the potential functions for this unique covalent modification of proteins.

UR - http://www.scopus.com/inward/record.url?scp=0023723998&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023723998&partnerID=8YFLogxK

M3 - Article

VL - 1

SP - 219

EP - 226

JO - BioFactors

JF - BioFactors

SN - 0951-6433

IS - 3

ER -