Abstract
An effector candidate for G protein action, GRIN1, was identified by screening a cDNA expression library with phosphorylated GTPgammaS-G(z)alpha as a probe. GRIN1 is a novel protein without substantial homology to known protein domains. It is expressed largely in brain and binds specifically to activated G(z)alpha, G(o)alpha, and G(i)alpha through its carboxyl-terminal region. The protein KIAA0514 (GRIN2) is homologous to GRIN1 at its carboxyl terminus and also binds to activated G(o)alpha. Both GRIN1 and G(o)alpha are membrane-bound proteins that are enriched in the growth cones of neurites. Coexpression of GRIN1 or GRIN2 with activated G(o)alpha causes formation of a network of fine processes in Neuro2a cells, suggesting that these pathways may function downstream of G(o)alpha to control growth of neurites.
Highlights
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF146569
Sequencing and data base searches revealed that Z-13 encoded the protein nucleobindin
Nucleobindin is described as a secreted protein that interacts with DNA [7]
Summary
GRIN1 is a novel protein without substantial homology to known protein domains It is expressed largely in brain and binds to activated Gz␣, Go␣, and Gi␣ through its carboxyl-terminal region. We have appended a site for phosphorylation by cyclic AMP-dependent protein kinase to the carboxyl terminus of Go␣; this region of G protein ␣ subunits is not involved in interactions with known effectors. This strategy led to isolation of a novel cDNA, initially designated Z-16, and detection of a homolog, KIAA0514. The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF146569
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