PMID- 10373502
OWN - NLM
STAT- MEDLINE
DCOM- 19990715
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 26
DP  - 1999 Jun 25
TI  - Amino-terminal cysteine residues of RGS16 are required for palmitoylation and
      modulation of Gi- and Gq-mediated signaling.
PG  - 18836-42
AB  - RGS proteins (Regulators of G protein Signaling) are a recently discovered family
      of proteins that accelerate the GTPase activity of heterotrimeric G protein alpha
      subunits of the i, q, and 12 classes. The proteins share a homologous core domain
      but have divergent amino-terminal sequences that are the site of palmitoylation
      for RGS-GAIP and RGS4. We investigated the function of palmitoylation for RGS16, 
      which shares conserved amino-terminal cysteines with RGS4 and RGS5. Mutation of
      cysteine residues at residues 2 and 12 blocked the incorporation of [3H]palmitate
      into RGS16 in metabolic labeling studies of transfected cells or into purified
      RGS proteins in a cell-free palmitoylation assay. The purified RGS16 proteins
      with the cysteine mutations were still able to act as GTPase-activating protein
      for Gialpha. Inhibition or a decrease in palmitoylation did not significantly
      change the amount of protein that was membrane-associated. However,
      palmitoylation-defective RGS16 mutants demonstrated impaired ability to inhibit
      both Gi- and Gq-linked signaling pathways when expressed in HEK293T cells. These 
      findings suggest that the amino-terminal region of RGS16 may affect the affinity 
      of these proteins for Galpha subunits in vivo or that palmitoylation localizes
      the RGS protein in close proximity to Galpha subunits on cellular membranes.
FAU - Druey, K M
AU  - Druey KM
AD  - Molecular Signal Transduction Section, Laboratory of Allergic Diseases, NIAID,
      National Institutes of Health, Bethesda, Maryland 20852, USA.
FAU - Ugur, O
AU  - Ugur O
FAU - Caron, J M
AU  - Caron JM
FAU - Chen, C K
AU  - Chen CK
FAU - Backlund, P S
AU  - Backlund PS
FAU - Jones, T L
AU  - Jones TL
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Palmitates)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proteins)
RN  - 0 (RGS Proteins)
RN  - 0 (RGS16 protein)
RN  - 0 (regulator of G-protein signalling 19)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gi-Go)
RN  - EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gq-G11)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Acylation
MH  - Animals
MH  - COS Cells
MH  - Chromatography, High Pressure Liquid
MH  - Consensus Sequence
MH  - Cysteine/*physiology
MH  - GTP-Binding Protein alpha Subunits, Gi-Go/*physiology
MH  - GTP-Binding Protein alpha Subunits, Gq-G11
MH  - GTP-Binding Proteins/*physiology
MH  - Guanosine Triphosphate/metabolism
MH  - Humans
MH  - Palmitates/*metabolism
MH  - Phosphoproteins/metabolism
MH  - Proteins/*metabolism
MH  - *RGS Proteins
MH  - *Signal Transduction
MH  - Transfection
EDAT- 1999/06/22 00:00
MHDA- 1999/06/22 00:01
CRDT- 1999/06/22 00:00
PHST- 1999/06/22 00:00 [pubmed]
PHST- 1999/06/22 00:01 [medline]
PHST- 1999/06/22 00:00 [entrez]
AID - 10.1074/jbc.274.26.18836 [doi]
AID - S0021-9258(19)87228-9 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Jun 25;274(26):18836-42. doi: 10.1074/jbc.274.26.18836.