PMID- 2105488
OWN - NLM
STAT- MEDLINE
DCOM- 19900306
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 87
IP  - 2
DP  - 1990 Jan
TI  - Myristoylation of an inhibitory GTP-binding protein alpha subunit is essential 
      for its membrane attachment.
PG  - 568-72
AB  - We transfected COS cells with cDNAs for the alpha subunits of stimulatory and 
      inhibitory GTP-binding proteins, alpha s and alpha i1, respectively, and 
      immunoprecipitated the metabolically labeled products with specific peptide 
      antibodies. Cells were separated into particulate and soluble fractions before 
      immunoprecipitation; [35S]methionine-labeled alpha s and alpha i were both found 
      primarily in the particulate fraction. [3H]Myristate was incorporated into 
      endogenous and transfected alpha i but could not be detected in alpha s even when 
      it was overexpressed. We converted the second residue, glycine, of alpha i1 into 
      alanine by site-directed mutagenesis. Upon transfection of the mutant alpha i1 
      into COS cells, the [35S]methionine-labeled product was localized primarily to 
      the soluble fraction, and, also unlike normal alpha i1, the mutant failed to 
      incorporate [3H]myristate. The unmyristoylated mutant alpha i1 could still 
      interact with the beta-gamma complex, since purified beta gamma subunits promoted 
      pertussis toxin-catalyzed ADP-ribosylation of both the normal and mutant alpha i1 
      subunits. These results indicate that myristoylation is critical for membrane 
      attachment of alpha i but not alpha s subunits.
FAU - Jones, T L
AU  - Jones TL
AD  - Molecular Pathophysiology Branch, National Institute of Diabetes and Digestive 
      and Kidney Disease, National Institutes of Health, Bethesda, MD 20892.
FAU - Simonds, W F
AU  - Simonds WF
FAU - Merendino, J J Jr
AU  - Merendino JJ Jr
FAU - Brann, M R
AU  - Brann MR
FAU - Spiegel, A M
AU  - Spiegel AM
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Hydroxylamines)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Myristic Acids)
RN  - 0 (Virulence Factors, Bordetella)
RN  - 0I3V7S25AW (Myristic Acid)
RN  - 0U46U6E8UK (NAD)
RN  - 20762-30-5 (Adenosine Diphosphate Ribose)
RN  - 2FP81O2L9Z (Hydroxylamine)
RN  - 9007-49-2 (DNA)
RN  - AE28F7PNPL (Methionine)
RN  - EC 2.4.2.31 (Pertussis Toxin)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Adenosine Diphosphate Ribose/metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cell Line
MH  - Cell Membrane/*metabolism
MH  - DNA/genetics
MH  - GTP-Binding Proteins/biosynthesis/genetics/*metabolism
MH  - Hydroxylamine
MH  - Hydroxylamines/pharmacology
MH  - Macromolecular Substances
MH  - Methionine/metabolism
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Myristic Acid
MH  - Myristic Acids/*metabolism
MH  - NAD/metabolism
MH  - Pertussis Toxin
MH  - *Protein Processing, Post-Translational
MH  - Transfection
MH  - Virulence Factors, Bordetella/metabolism
PMC - PMC53306
EDAT- 1990/01/01 00:00
MHDA- 2001/03/28 10:01
PMCR- 1990/07/01
CRDT- 1990/01/01 00:00
PHST- 1990/01/01 00:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1990/01/01 00:00 [entrez]
PHST- 1990/07/01 00:00 [pmc-release]
AID - 10.1073/pnas.87.2.568 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1990 Jan;87(2):568-72. doi: 10.1073/pnas.87.2.568.