PMID- 10339594
OWN - NLM
STAT- MEDLINE
DCOM- 19990624
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 11
DP  - 1999 May 25
TI  - Interaction between RGS7 and polycystin.
PG  - 6371-6
AB  - Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase 
      activity of certain Galpha subunits and thereby modulate a number of G
      protein-dependent signaling cascades. Currently, little is known about the
      regulation of RGS proteins themselves. We identified a short-lived RGS protein,
      RGS7, that is rapidly degraded through the proteasome pathway. The degradation of
      RGS7 is inhibited by interaction with a C-terminal domain of polycystin, the
      protein encoded by PKD1, a gene involved in autosomal-dominant polycystic kidney 
      disease. Furthermore, membranous expression of C-terminal polycystin relocalized 
      RGS7. Our results indicate that rapid degradation and interaction with integral
      membrane proteins are potential means of regulating RGS proteins.
FAU - Kim, E
AU  - Kim E
AD  - Laboratory of Molecular and Developmental Neuroscience, Massachusetts General
      Hospital, Harvard Medical School, Boston, MA 02114, USA.
FAU - Arnould, T
AU  - Arnould T
FAU - Sellin, L
AU  - Sellin L
FAU - Benzing, T
AU  - Benzing T
FAU - Comella, N
AU  - Comella N
FAU - Kocher, O
AU  - Kocher O
FAU - Tsiokas, L
AU  - Tsiokas L
FAU - Sukhatme, V P
AU  - Sukhatme VP
FAU - Walz, G
AU  - Walz G
LA  - eng
SI  - GENBANK/AF090116
SI  - GENBANK/AF090117
GR  - MH01147/MH/NIMH NIH HHS/United States
GR  - R01 DK52897/DK/NIDDK NIH HHS/United States
GR  - R01-DK51060/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
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 (Multienzyme Complexes)
RN  - 0 (Proteins)
RN  - 0 (RGS Proteins)
RN  - 0 (RGS7 protein, human)
RN  - 0 (Recombinant Proteins)
RN  - 0 (TRPP Cation Channels)
RN  - 0 (Ubiquitins)
RN  - 0 (polycystic kidney disease 1 protein)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
RN  - EC 3.4.25.1 (Proteasome Endopeptidase Complex)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - B-Lymphocytes/metabolism
MH  - Binding Sites
MH  - Cysteine Endopeptidases/metabolism
MH  - GTP-Binding Proteins/chemistry/metabolism
MH  - Gene Library
MH  - Humans
MH  - Molecular Sequence Data
MH  - Multienzyme Complexes/metabolism
MH  - Polycystic Kidney, Autosomal Dominant/genetics/metabolism
MH  - Proteasome Endopeptidase Complex
MH  - Protein Biosynthesis
MH  - Proteins/chemistry/*genetics/*metabolism
MH  - *RGS Proteins
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Saccharomyces cerevisiae
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - TRPP Cation Channels
MH  - Transcription, Genetic
MH  - Ubiquitins/metabolism
PMC - PMC26888
EDAT- 1999/05/26 00:00
MHDA- 1999/05/26 00:01
CRDT- 1999/05/26 00:00
PHST- 1999/05/26 00:00 [pubmed]
PHST- 1999/05/26 00:01 [medline]
PHST- 1999/05/26 00:00 [entrez]
AID - 10.1073/pnas.96.11.6371 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 May 25;96(11):6371-6. doi:
      10.1073/pnas.96.11.6371.