PMID- 10022914
OWN - NLM
STAT- MEDLINE
DCOM- 19990325
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 3
DP  - 1999 Mar
TI  - Identification of a novel family of targets of PYK2 related to Drosophila retinal
      degeneration B (rdgB) protein.
PG  - 2278-88
AB  - The protein tyrosine kinase PYK2 has been implicated in signaling pathways
      activated by G-protein-coupled receptors, intracellular calcium, and stress
      signals. Here we describe the molecular cloning and characterization of a novel
      family of PYK2-binding proteins designated Nirs (PYK2 N-terminal
      domain-interacting receptors). The three Nir proteins (Nir1, Nir2, and Nir3) bind
      to the amino-terminal domain of PYK2 via a conserved sequence motif located in
      the carboxy terminus. The primary structures of Nirs reveal six putative
      transmembrane domains, a region homologous to phosphatidylinositol (PI) transfer 
      protein, and an acidic domain. The Nir proteins are the human homologues of the
      Drosophila retinal degeneration B protein (rdgB), a protein implicated in the
      visual transduction pathway in flies. We demonstrate that Nirs are
      calcium-binding proteins that exhibit PI transfer activity in vivo. Activation of
      PYK2 by agents that elevate intracellular calcium or by phorbol ester induce
      tyrosine phosphorylation of Nirs. Moreover, PYK2 and Nirs exhibit similar
      expression patterns in several regions of the brain and retina. In addition,
      PYK2-Nir complexes are detected in lysates prepared from cultured cells or from
      brain tissues. Finally, the Nir1-encoding gene is located at human chromosome
      17p13.1, in proximity to a locus responsible for several human retinal diseases. 
      We propose that the Nir and rdgB proteins represent a new family of
      evolutionarily conserved PYK2-binding proteins that play a role in the control of
      calcium and phosphoinositide metabolism downstream of G-protein-coupled
      receptors.
FAU - Lev, S
AU  - Lev S
AD  - Sugen, Inc., South San Francisco, California 94080, USA.
FAU - Hernandez, J
AU  - Hernandez J
FAU - Martinez, R
AU  - Martinez R
FAU - Chen, A
AU  - Chen A
FAU - Plowman, G
AU  - Plowman G
FAU - Schlessinger, J
AU  - Schlessinger J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Eye Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (PITPNM1 protein, human)
RN  - 0 (PITPNM2 protein, human)
RN  - 0 (PITPNM3 protein, human)
RN  - 139135-48-1 (rdgB protein, Drosophila)
RN  - 42HK56048U (Tyrosine)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Focal Adhesion Kinase 2)
RN  - EC 2.7.10.2 (Ptk2b protein, rat)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Brain/metabolism
MH  - Calcium/metabolism
MH  - Calcium-Binding Proteins/genetics/*metabolism
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - *Drosophila Proteins
MH  - Drosophila melanogaster
MH  - *Eye Proteins
MH  - Focal Adhesion Kinase 2
MH  - Humans
MH  - Membrane Proteins/*chemistry
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - Protein-Tyrosine Kinases/*metabolism
MH  - Rabbits
MH  - Rats
MH  - Retina/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
MH  - Tyrosine/metabolism
PMC - PMC84020
EDAT- 1999/02/18 00:00
MHDA- 1999/02/18 00:01
CRDT- 1999/02/18 00:00
PHST- 1999/02/18 00:00 [pubmed]
PHST- 1999/02/18 00:01 [medline]
PHST- 1999/02/18 00:00 [entrez]
AID - 10.1128/mcb.19.3.2278 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Mar;19(3):2278-88. doi: 10.1128/mcb.19.3.2278.