Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies

Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic cells and regulates numerous biological pathways, such as membrane trafficking, protein secretion, signal trans...

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Published inChemical reviews Vol. 118; no. 3; pp. 919 - 988
Main Authors Jiang, Hong, Zhang, Xiaoyu, Chen, Xiao, Aramsangtienchai, Pornpun, Tong, Zhen, Lin, Hening
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 14.02.2018
Subjects
Acylation
Alkyl and Aryl Transferases - antagonists & inhibitors
Alkyl and Aryl Transferases - chemistry
Alkyl and Aryl Transferases - metabolism
Animals
Apoptosis
cell membranes
Cysteine
enzymes
Eukaryotes
eukaryotic cells
Glycine
Humans
Kinetics
Lipids
Lysine
Myristic Acids - metabolism
myristoylation
Palmitic Acids - metabolism
palmitoylation
physiological transport
Protein Interaction Maps
Protein Prenylation
protein secretion
Proteins
Proteins - chemistry
Proteins - metabolism
serine
Signal transduction
Substrate Specificity
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Abstract Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic cells and regulates numerous biological pathways, such as membrane trafficking, protein secretion, signal transduction, and apoptosis. We provide a comprehensive review of protein lipidation, including descriptions of proteins known to be modified and the functions of the modifications, the enzymes that control them, and the tools and technologies developed to study them. We also highlight key questions about protein lipidation that remain to be answered, the challenges associated with answering such questions, and possible solutions to overcome these challenges.
AbstractList Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic cells and regulates numerous biological pathways, such as membrane trafficking, protein secretion, signal transduction, and apoptosis. We provide a comprehensive review of protein lipidation, including descriptions of proteins known to be modified and the functions of the modifications, the enzymes that control them, and the tools and technologies developed to study them. We also highlight key questions about protein lipidation that remain to be answered, the challenges associated with answering such questions, and possible solutions to overcome these challenges.
Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic cells and regulates numerous biological pathways, such as membrane trafficking, protein secretion, signal transduction, and apoptosis. We provide a comprehensive review of protein lipidation, including descriptions of proteins known to be modified and the functions of the modifications, the enzymes that control them, and the tools and technologies developed to study them. We also highlight key questions about protein lipidation that remain to be answered, the challenges associated with answering such questions, and possible solutions to overcome these challenges.Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic cells and regulates numerous biological pathways, such as membrane trafficking, protein secretion, signal transduction, and apoptosis. We provide a comprehensive review of protein lipidation, including descriptions of proteins known to be modified and the functions of the modifications, the enzymes that control them, and the tools and technologies developed to study them. We also highlight key questions about protein lipidation that remain to be answered, the challenges associated with answering such questions, and possible solutions to overcome these challenges.
Author Lin, Hening
Jiang, Hong
Chen, Xiao
Aramsangtienchai, Pornpun
Tong, Zhen
Zhang, Xiaoyu
AuthorAffiliation Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology
AuthorAffiliation_xml – name: Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology
Author_xml – sequence: 1
  givenname: Hong
  surname: Jiang
  fullname: Jiang, Hong
– sequence: 2
  givenname: Xiaoyu
  surname: Zhang
  fullname: Zhang, Xiaoyu
– sequence: 3
  givenname: Xiao
  surname: Chen
  fullname: Chen, Xiao
– sequence: 4
  givenname: Pornpun
  surname: Aramsangtienchai
  fullname: Aramsangtienchai, Pornpun
– sequence: 5
  givenname: Zhen
  surname: Tong
  fullname: Tong, Zhen
– sequence: 6
  givenname: Hening
  orcidid: 0000-0002-0255-2701
  surname: Lin
  fullname: Lin, Hening
  email: hl379@cornell.edu
BackLink https://www.ncbi.nlm.nih.gov/pubmed/29292991$$D View this record in MEDLINE/PubMed
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Snippet Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine palmitoylation, and serine and lysine fatty acylation, occurs...
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SubjectTerms Acylation
Alkyl and Aryl Transferases - antagonists & inhibitors
Alkyl and Aryl Transferases - chemistry
Alkyl and Aryl Transferases - metabolism
Animals
Apoptosis
cell membranes
Cysteine
enzymes
Eukaryotes
eukaryotic cells
Glycine
Humans
Kinetics
Lipids
Lysine
Myristic Acids - metabolism
myristoylation
Palmitic Acids - metabolism
palmitoylation
physiological transport
Protein Interaction Maps
Protein Prenylation
protein secretion
Proteins
Proteins - chemistry
Proteins - metabolism
serine
Signal transduction
Substrate Specificity
Title Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies
URI http://dx.doi.org/10.1021/acs.chemrev.6b00750
https://www.ncbi.nlm.nih.gov/pubmed/29292991
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https://www.proquest.com/docview/2131894927
https://pubmed.ncbi.nlm.nih.gov/PMC5985209
Volume 118
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