Two variants of MutS homolog hMSH5: Prevalence in humans and effects on protein interaction

Yi, Wei; Wu, Xiaopan; Lee, Tai-Hsien; Doggett, Norman A.; Her, Chengtao

doi:10.1016/j.bbrc.2005.04.154

Cited by 31 publications

(64 citation statements)

References 12 publications

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“…The pPuro-FLAG vector [10] was used to generate mammalian expression constructs pPuro-FLAG/hMRE11 and pPuro-FLAG/hMRE11 . Full-length hMLH1 cDNA was cloned into pcDNA6 (Invitrogen, Carlsbad, CA) to create the mammalian expression construct pcDNA6/hMLH1.…”

Section: Cell Lines and Transfectionmentioning

confidence: 99%

The interplay between hMLH1 and hMRE11: Role in MMR and the effect of hMLH1 mutations

Zhao

Zhu

Yuan

et al. 2008

Biochemical and Biophysical Research Communications

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Our previous studies indicate that hMRE11 plays a role in MMR, and this function of hMRE11 is most likely mediated by the hMLH1-hMRE11 interaction. Here, we explored the functional implications of the hMLH1-hMRE11 interaction in MMR and the effects of hMLH1 mutations on their interaction. Our in vitro MMR assay demonstrated that the dominant-negative hMRE11 452-634 mutant peptide (i.e., harboring only the hMLH1-interacting domain) imparted a significant reduction in both 3' excision and 3'-directed MMR activities. Furthermore, the expression of hMRE11 , and to a lesser extent hMRE11 1-634 (ATLD1), impaired G2/M checkpoint control in response to MNU and cisplatin treatments, rendering cells resistant to killings by these two anticancer drugs. Analysis of 38 hMLH1 missense mutations showed that the majority of mutations caused significant (> 50%) reductions in their interaction with hMRE11, suggesting a potential link between aberrant protein interaction and the pathogenic effects of hMLH1 variants.

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Section: Cell Lines and Transfectionmentioning

confidence: 99%

The interplay between hMLH1 and hMRE11: Role in MMR and the effect of hMLH1 mutations

Zhao

Zhu

Yuan

et al. 2008

Biochemical and Biophysical Research Communications

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“…This study provided evidence that the PMS2 Ser775Asn variant attenuates the binding of MLH1 and PMS2 detected by fluorescence resonance energy transfer (FRET) and co-immunoprecipitation assay, further supporting the potential interaction between MLH1-PMS2 and MLH1-MLH3 discussed above. The MSH5 Pro29Ser polymorphism is located within the MSH4-MSH5 interacting domain and leads to a weakened formation of the MSH4-MSH5 heterocomplex (Yi et al, 2005). This was supported by the study of Xu et al (2010).…”

Section: Mmr Alterations and Infertilitymentioning

confidence: 86%

Impact of DNA mismatch repair system alterations on human fertility and related treatments

Liu

Wang

et al. 2016

J. Zhejiang Univ. Sci. B

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DNA mismatch repair (MMR) is one of the biological pathways, which plays a critical role in DNA homeostasis, primarily by repairing base-pair mismatches and insertion/deletion loops that occur during DNA replication. MMR also takes part in other metabolic pathways and regulates cell cycle arrest. Defects in MMR are associated with genomic instability, predisposition to certain types of cancers and resistance to certain therapeutic drugs. Moreover, genetic and epigenetic alterations in the MMR system demonstrate a significant relationship with human fertility and related treatments, which helps us to understand the etiology and susceptibility of human infertility. Alterations in the MMR system may also influence the health of offspring conceived by assisted reproductive technology in humans. However, further studies are needed to explore the specific mechanisms by which the MMR system may affect human infertility. This review addresses the physiological mechanisms of the MMR system and associations between alterations of the MMR system and human fertility and related treatments, and potential effects on the next generation.

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“…The hMSH5 gene produces multiple alternative transcripts, of which four hMSH5 variants that maintain the reading frame have been identified (hMSH5a, hMSH5b, hMSH5c, and hMSH5d; UniGene database) and hMSH5c appears to be identical to that of the originally described human hMSH5. Referenced by the deduced amino acid sequence of hMSH5, it is evident that hMSH5a (hMSH5sv) encodes an 851-amino acid protein containing a 17-amino acid insertion between codons 179 and 180, owing to the retention of the last 51-bp of hMSH5 intron 6 (Yi et al 2005), whereas hMSH5b harbors one extra amino acid residue between codons 654 and 655-due to the retention of the last 3 nucleotides of hMSH5 intron 20 (Her & Doggett 1998). hMSH5d represents the shortest hMSH5 variant.…”

Section: Splicing Variants and Nonsynonymous Polymorphisms Of Hmsh4 Amentioning

confidence: 99%

The Role of MutS Homologues MSH4 and MSH5 in DNA Metabolism and Damage Response

Wu¹,

Xu²,

Her³

2011

DNA Replication and Related Cellular Processes

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Two variants of MutS homolog hMSH5: Prevalence in humans and effects on protein interaction

Cited by 31 publications

References 12 publications

The interplay between hMLH1 and hMRE11: Role in MMR and the effect of hMLH1 mutations

The interplay between hMLH1 and hMRE11: Role in MMR and the effect of hMLH1 mutations

Impact of DNA mismatch repair system alterations on human fertility and related treatments

The Role of MutS Homologues MSH4 and MSH5 in DNA Metabolism and Damage Response

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