ArticleJournal of molecular neuroscience : MN1996
CR16, a novel proline-rich protein expressed in rat brain neurons, binds to SH3 domains and is a MAP kinase substrate.
Article in Journal of molecular neuroscience : MN, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 28 citations in OpenAlex.
- Identification of shared mechanisms between Alzheimer's disease and atherosclerosis by integrated bioinformatics analysis.European journal of medical research · 2025Article
- MoVrp1, a putative verprolin protein, is required for asexual development and infection in the rice blast fungus Magnaporthe oryzae.Scientific reports · 2017Article
- The enteropathogenic E. coli effector EspH promotes actin pedestal formation and elongation via WASP-interacting protein (WIP).Cellular microbiology · 2012Article
- WIP remodeling actin behind the scenes: how WIP reshapes immune and other functions.International journal of molecular sciences · 2012Review
- The formin-homology protein SmDia interacts with the Src kinase SmTK and the GTPase SmRho1 in the gonads of Schistosoma mansoni.PloS one · 2009Article
- CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
CR16 is a glucocorticoid-regulated gene expressed in subpopulations of neurons in the brain, including the hippocampus. The CR16 open reading frame encodes a 45 kDa protein containing 32% proline. To begin characterizing the CR16 protein, a rabbit polyclonal antibody was raised against an Escherchia coli-produced fusion protein containing amino acids 370-438 of CR16. The antibody identifies a protein doublet of 68 and 72 kDa by sodium-dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) from hippocampal extracts and from insect cells expressing the CR16 open reading frame from a baculovirus construct. However, when hippocampal extracts are electrophoresed on nondenaturing polyacrylamide gels, the CR16 protein migrates as a 48 kDa protein that better correlates with the size of the open reading frame. Examination of the primary amino acid sequence reveals at least 12 sequence homologies to the abl-SH3 binding domain consensus sequence XPXXPPP psi XP. In addition, CR16 has at least 36 copies of the PXXP motif, which is contained in all known SH3 binding domains. Solution and filter binding assays confirm that CR16 selectively binds SH3 domains. The CR16 primary amino acid sequence also contains at least eight consensus MAP kinase phosphorylation sites, five of which are in the potential SH3 binding domains. The CR16 protein, immunoprecipitated from rat brain, is an in vitro substrate for the purified enzyme. However, phosphorylation of CR16 does not greatly affect the binding of the various SH3 domains in our assay system. These data strongly suggest that the function of CR16 is to mediate one or more signal transduction pathways in CNS neurons, in addition to being a glucocorticoid-regulated gene.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.