Two classes of fatty acid acylated proteins exist in eukaryotic cells.

A. I. Magee, Sara Courtneidge

Research output: Contribution to journalArticle

85 Citations (Scopus)

Abstract

Labelling of cultured cells with [3H]palmitic and [3H]myristic acids demonstrates that each of these fatty acids modifies a substantially different subset of cellular proteins. Hydroxylamine treatment can be used to differentiate sensitive thioester linkages to palmitate from insensitive amide linkages to myristate. Several palmitoylated proteins are surface-oriented glycoproteins while all of the myristylated proteins appear to be internal. Myristate addition is much more tightly coupled to protein synthesis than palmitoylation, which is able to continue at a reduced level even in the prolonged absence of protein synthesis. Acyl proteins patterns were affected both qualitatively and quantitatively by transformation and growth status. The preferential addition of palmitate to the transferrin receptor and myristate to pp60src, and the absence of these modifications from several other proteins is reported. We propose a nomenclature for fatty acyl proteins based on these observations.

Original languageEnglish (US)
Pages (from-to)1137-1144
Number of pages8
JournalEMBO Journal
Volume4
Issue number5
StatePublished - May 1985
Externally publishedYes

Fingerprint

Eukaryotic Cells
Fatty Acids
Myristic Acid
Proteins
Palmitates
Myristic Acids
Lipoylation
Hydroxylamine
Transferrin Receptors
Terminology
Membrane Glycoproteins
Amides
Labeling
Glycoproteins
Membrane Proteins
Cultured Cells
Cells
Growth

ASJC Scopus subject areas

  • Cell Biology
  • Genetics

Cite this

Two classes of fatty acid acylated proteins exist in eukaryotic cells. / Magee, A. I.; Courtneidge, Sara.

In: EMBO Journal, Vol. 4, No. 5, 05.1985, p. 1137-1144.

Research output: Contribution to journalArticle

@article{1bec422e8dd245718cfd01b5fdbaae3b,
title = "Two classes of fatty acid acylated proteins exist in eukaryotic cells.",
abstract = "Labelling of cultured cells with [3H]palmitic and [3H]myristic acids demonstrates that each of these fatty acids modifies a substantially different subset of cellular proteins. Hydroxylamine treatment can be used to differentiate sensitive thioester linkages to palmitate from insensitive amide linkages to myristate. Several palmitoylated proteins are surface-oriented glycoproteins while all of the myristylated proteins appear to be internal. Myristate addition is much more tightly coupled to protein synthesis than palmitoylation, which is able to continue at a reduced level even in the prolonged absence of protein synthesis. Acyl proteins patterns were affected both qualitatively and quantitatively by transformation and growth status. The preferential addition of palmitate to the transferrin receptor and myristate to pp60src, and the absence of these modifications from several other proteins is reported. We propose a nomenclature for fatty acyl proteins based on these observations.",
author = "Magee, {A. I.} and Sara Courtneidge",
year = "1985",
month = "5",
language = "English (US)",
volume = "4",
pages = "1137--1144",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "5",

}

TY - JOUR

T1 - Two classes of fatty acid acylated proteins exist in eukaryotic cells.

AU - Magee, A. I.

AU - Courtneidge, Sara

PY - 1985/5

Y1 - 1985/5

N2 - Labelling of cultured cells with [3H]palmitic and [3H]myristic acids demonstrates that each of these fatty acids modifies a substantially different subset of cellular proteins. Hydroxylamine treatment can be used to differentiate sensitive thioester linkages to palmitate from insensitive amide linkages to myristate. Several palmitoylated proteins are surface-oriented glycoproteins while all of the myristylated proteins appear to be internal. Myristate addition is much more tightly coupled to protein synthesis than palmitoylation, which is able to continue at a reduced level even in the prolonged absence of protein synthesis. Acyl proteins patterns were affected both qualitatively and quantitatively by transformation and growth status. The preferential addition of palmitate to the transferrin receptor and myristate to pp60src, and the absence of these modifications from several other proteins is reported. We propose a nomenclature for fatty acyl proteins based on these observations.

AB - Labelling of cultured cells with [3H]palmitic and [3H]myristic acids demonstrates that each of these fatty acids modifies a substantially different subset of cellular proteins. Hydroxylamine treatment can be used to differentiate sensitive thioester linkages to palmitate from insensitive amide linkages to myristate. Several palmitoylated proteins are surface-oriented glycoproteins while all of the myristylated proteins appear to be internal. Myristate addition is much more tightly coupled to protein synthesis than palmitoylation, which is able to continue at a reduced level even in the prolonged absence of protein synthesis. Acyl proteins patterns were affected both qualitatively and quantitatively by transformation and growth status. The preferential addition of palmitate to the transferrin receptor and myristate to pp60src, and the absence of these modifications from several other proteins is reported. We propose a nomenclature for fatty acyl proteins based on these observations.

UR - http://www.scopus.com/inward/record.url?scp=0022065554&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022065554&partnerID=8YFLogxK

M3 - Article

VL - 4

SP - 1137

EP - 1144

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 5

ER -