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Gene Review

MSH5  -  mutS homolog 5

Homo sapiens

Synonyms: G7, MUTSH5, MutS protein homolog 5, NG23, hMSH5
 
 
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High impact information on MSH5

  • Here, we demonstrate that purified hMSH4-hMSH5 binds uniquely to Holliday Junctions [1].
  • Our data also indicate that the hMSH5 P29S variant overactivates the c-Abl tyrosine kinase activity [2].
  • Here, we report a novel physical and functional interaction between hMSH5 and c-Abl; the latter is a critical non-receptor tyrosine kinase involved in many critical cellular functions including DNA damage response, in which the kinase activity is normally suppressed in the absence of biological challenges [2].
  • This physical interaction facilitates the activation of c-Abl tyrosine kinase and the phosphorylation of hMSH5 in response to ionizing radiation [2].
  • Our data indicate that hMSH5 associates with c-Abl in vivo, which is mediated by a direct physical interaction between the NH2 terminus (residues 1-109) of hMSH5 and the c-Abl SH3 domain [2].
 

Biological context of MSH5

  • MSH5 is known to play functional roles in an array of cellular processes such as DNA damage response and meiotic homologous recombination [3].
  • hMSH5: a human MutS homologue that forms a novel heterodimer with hMSH4 and is expressed during spermatogenesis [4].
  • hMSH4-hMSH5 recognizes Holliday Junctions and forms a meiosis-specific sliding clamp that embraces homologous chromosomes [1].
  • Haplotype analysis and direct sequencing failed to show involvement of the known mismatch repair genes, with the exception of MSH5, in this kindred [5].
  • Analysis of large fragments (from 3.9 to 6. 2 kb) covering the entire 25 kb MSH5 gene in the proband revealed the absence of gross changes in the promoter region and exons [5].
 

Associations of MSH5 with chemical compounds

  • We have also identified an hMSH5 polymorphism (C85T) [corrected] that altered codon 29 of the hMSH5 gene resulting in a proline-to-serine change (P29S) [3].
 

Physical interactions of MSH5

  • Three-hybrid analysis suggested that VBP1 could compete with hMSH5 for the binding of hMSH4 [6].
 

Regulatory relationships of MSH5

 

Other interactions of MSH5

  • Mammalian MSH4 and MSH5 proteins form a heterodimeric complex and play an important role in the meiotic processes [6].
  • The protein encoded by hMSH4sv was unable to interact with hMSH5, but it retained the capacity to interact with VBP1 [6].
  • Formation of hMSH4-hMSH5 heterocomplex is a prerequisite for subsequent GPS2 recruitment [7].
  • Mutation of TM3 residues D122 and D126 and TM6 residues F261 and H264 decreased the binding affinity of NDP-MSH 5-fold or greater, thereby identifying these receptor residues as sites potentially involved in the sought after ligand-receptor interactions [8].

References

  1. hMSH4-hMSH5 recognizes Holliday Junctions and forms a meiosis-specific sliding clamp that embraces homologous chromosomes. Snowden, T., Acharya, S., Butz, C., Berardini, M., Fishel, R. Mol. Cell (2004) [Pubmed]
  2. Physical and functional interaction between hMSH5 and c-Abl. Yi, W., Lee, T.H., Tompkins, J.D., Zhu, F., Wu, X., Her, C. Cancer Res. (2006) [Pubmed]
  3. Two variants of MutS homolog hMSH5: prevalence in humans and effects on protein interaction. Yi, W., Wu, X., Lee, T.H., Doggett, N.A., Her, C. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  4. hMSH5: a human MutS homologue that forms a novel heterodimer with hMSH4 and is expressed during spermatogenesis. Bocker, T., Barusevicius, A., Snowden, T., Rasio, D., Guerrette, S., Robbins, D., Schmidt, C., Burczak, J., Croce, C.M., Copeland, T., Kovatich, A.J., Fishel, R. Cancer Res. (1999) [Pubmed]
  5. Probable involvement of a germ-line mutation of an unknown mismatch repair gene in a Japanese Muir-Torre syndrome phenotype. Kubota, T., Dakeishi, M., Nozaki, J., Manabe, M., Koizumi, A. J. Dermatol. Sci. (2000) [Pubmed]
  6. Human MutS homologue MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1. Her, C., Wu, X., Griswold, M.D., Zhou, F. Cancer Res. (2003) [Pubmed]
  7. Formation of hMSH4-hMSH5 heterocomplex is a prerequisite for subsequent GPS2 recruitment. Lee, T.H., Yi, W., Griswold, M.D., Zhu, F., Her, C. DNA Repair (Amst.) (2006) [Pubmed]
  8. Molecular determinants of ligand binding to the human melanocortin-4 receptor. Yang, Y.K., Fong, T.M., Dickinson, C.J., Mao, C., Li, J.Y., Tota, M.R., Mosley, R., Van Der Ploeg, L.H., Gantz, I. Biochemistry (2000) [Pubmed]
 
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