High impact information on CSRP1

• At the N-terminus restrictin contains a cysteine-rich segment of about 140 aa that might link restrictin monomers into oligomers [1].
• One strategy for defining the mechanism by which CRPs potentiate myogenesis is to characterize the repertoire of CRP binding partners [2].
• We have performed quantitative Western immunoblot analysis of cCRP, zyxin, and alpha-actinin levels during embryogenesis [3].
• In primary cell cultures derived from embryonic gizzard, differentiated smooth muscle cells exhibit the most striking staining with anti-cCRP antibodies [3].
• Molecular characterization of the VLDL/VTGR revealed that it is a member of the LDLR gene superfamily, and harbours eight complement-type, cysteine-rich ligand binding repeats at the N-terminus [4].

Biological context of CSRP1

• Members of the cysteine-rich protein (CRP) family are evolutionarily conserved proteins that have been implicated in the processes of cell proliferation and differentiation [5].
• Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression [5].
• In this study, we have addressed the biological significance of the CRP multigene family by comparing the subcellular distributions, biochemical properties, and expression patterns of CRP1, CRP2, and CRP3/MLP [5].
• Collectively, our results suggest that the binding site for zyxin on CRP1 is not contained within a single contiguous sequence of amino acids [6].
• Previous studies have demonstrated that the adhesion-plaque protein, zyxin, interacts specifically with a 23 kDa protein, called the cysteine-rich protein 1 (CRP1), which has been implicated in myogenesis [6].

Anatomical context of CSRP1

• Our data reveal that all three CRP family members, when expressed in adherent fibroblasts, associate specifically with the actin cytoskeleton [5].
• The demonstration that all members of the CRP family are associated with cytoskeletal components that have been implicated in the assembly and organization of filamentous actin suggests that CRPs contribute to muscle cell differentiation via effects on cytoarchitecture [5].
• In particular, one CRP family member has been shown to be an essential regulator of cardiac and skeletal muscle development [5].
• RESULTS: CRP1 expression increased actin bundling in rat embryonic fibroblasts [7].
• Cysteine-rich protein 1 (CRP1) regulates actin filament bundling [7].

Associations of CSRP1 with chemical compounds

• Each of the three vertebrate CRP isoforms characterized to date is composed of two copies of the zinc-binding LIM domain with associated glycine-rich repeats [5].
• Mutant receptor proteins which retained the highly conserved cysteine-rich (C1) region were able to bind to DNA-cellulose, although removal of 290 amino acids from the C-terminus resulted in reduced affinity for DNA [8].
• The deduced amino acid sequence comprises a cysteine-rich extracellular domain, a single hydrophobic transmembrane domain, and a cytoplasmic serine/threonine kinase domain [9].
• Precursor-product relationship between chicken vitellogenin and the yolk proteins: the 40 kDa yolk plasma glycoprotein is derived from the C-terminal cysteine-rich domain of vitellogenin II [10].

Physical interactions of CSRP1

• Moreover, all three CRP isoforms are capable of interacting with the cytoskeletal proteins alpha-actinin and zyxin [5].

Other interactions of CSRP1

• It closely resembles the mammalian so-called very low density lipoprotein receptors, in that its aminoterminal ligand binding domain consists of a cluster of 8 cysteine-rich repeats [11].

Analytical, diagnostic and therapeutic context of CSRP1

• Examination of a number of chick embryonic tissues by Western immunoblot analysis reveals that cCRP exhibits tissue-specific expression. cCRP is most prominent in tissues that are enriched in smooth muscle cells, such as gizzard, stomach, and intestine [3].
• Primary sequence analyses have revealed that both zyxin and CRP1 exhibit multiple copies of a structural motif called the LIM domain [6].

References