Disease relevance of S100a10

• A polypeptide (p10), corresponding to this domain, has been synthesized by means of an Escherichia coli expression system and purified to homogeneity [1].
• We now report that antiserum directed against rat type C virus p15, but not viral p12, p10, or p27, immunoprecipitated rat sarcoma virus p29 [2].
• A novel approach to construct a single recombinant baculovirus expressing two protein subunits simultaneously by replacing polyhedrin as well as p10 coding sequences is described [3].

High impact information on S100a10

• The endogenous Na(V)1.8 current in sensory neurons is inhibited by antisense downregulation of p11 expression [4].
• T42A-Ran.GDP also retains the ability to bind p10/NTF2, a component of the nuclear import pathway [5].
• In contrast, the fluorescently labeled, 890-nucleotide-long viral RNA segment does not dock to the nuclear envelope or enter the nucleus either in the presence of exogenous cytosol or of karyopherin heterodimer, Ran, and p10 [6].
• Taken together, our results suggest that the HD is involved in both syncytium formation and in determining p10 transport and surface expression [7].
• In contrast to the CTL responses, plasmid vaccination was a poor inducer of an antibody response to p10 [8].

Biological context of S100a10

• 9. The binding of amino acids 74-103 of Na(V)1.8 to p11 residues 33-78 occurs in a random coiled region flanked by two EF hand motifs whose crystal structure has been established [9].
• Two codominant p10 epitopes, M(1)SSDLRLTLL(10) and T(8)LLELVRRL(16), associated with the RT1.A(l) major histocompatibility complex class I molecules of the Lewis rats, were identified [8].
• Characterization and properties of a protein kinase associated with murine sarcoma-leukemia virus (MSV-MuLV). Endogenous phosphorylation of a unique p10 polypeptide [10].

Physical interactions of S100a10

• Here we show that p11 binds to Na(V)1.8 but not to sodium channel isoforms Na(V)1.2, 1.5, 1.7 or Na(V)1 [9].

Other interactions of S100a10

• Because direct association with p11 is required for functional expression of Na(V)1.8, disrupting this interaction may be a useful new approach to downregulating Na(V)1.8 and effecting analgesia [4].
• The interaction of p11 (annexin II light chain) with the N-terminal domain of Na(V)1.8, a tetrodotoxin-resistant sodium channel, is essential for the functional expression of the channel [9].

Analytical, diagnostic and therapeutic context of S100a10

• Circular dichroism technique also shows that the interaction of p10 with RNA involves an unstacking of the nucleotide bases and an unfolding of the RNA secondary structure [1].
• Sequence analysis and structural studies identified p10 as a type I membrane protein with a central transmembrane domain, a cytoplasmic basic region, and an N-terminal hydrophobic domain (HD) that was hypothesized to function as a fusion peptide [7].
• A direct comparison of SSAV p10 and the cleavage product SSV p10 by SDS-PAGE suggests that SSAV pr65gag and SSV p65 differ slightly by molecular weight [11].

References