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DUSP16  -  dual specificity phosphatase 16

Homo sapiens

Synonyms: Dual specificity protein phosphatase 16, KIAA1700, MAP kinase phosphatase 7, MKP-7, MKP7, ...
 
 
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High impact information on DUSP16

 

Biological context of DUSP16

  • Taken together, the functional data point to a context-dependent role for DUSP16 on cell transformation and apoptosis, reflecting the dual role of JNK, and therefore suggest that DUSP16 might be haploinsufficient for tumor suppression [4].
  • Phosphorylation of Ser-446 determines stability of MKP-7 [2].
  • In the present study, we have identified a novel MKP, designated MKP-7, and mapped it to human chromosome 12p12 [5].
  • When expressed in mammalian cells MKP-7 protein was localized exclusively in the cytoplasm, but this localization became exclusively nuclear following leptomycin B treatment or introduction of a mutation in the nuclear export signal [5].
 

Anatomical context of DUSP16

  • However, no inactivating mutations could be detected in leukemia patients hemizygous for DUSP16, and the effect of hemizygosity on DUSP16 expression level could not be assessed due to the variability of DUSP16 transcript levels observed in leukaemia cell lines and in patients [4].
  • MKP-7 is predominantly localized in the cytoplasm when expressed in cultured cells, whereas hVH5 is both in the nucleus and the cytoplasm [6].
  • In this study we found that, when expressed in COS-7 cells with HA-ERK2, the mobility of FLAG-MKP-7 was decreased on SDS-PAGE gels depending on several stimuli, including phorbol 12-myristate 13-acetate, fetal bovine serum, epidermal growth factor, H2O2, and ionomycin [3].
 

Associations of DUSP16 with chemical compounds

  • These findings indicate that MKP-7 is the first identified leptomycin B-sensitive shuttle MKP [5].
 

Physical interactions of DUSP16

 

Other interactions of DUSP16

  • A role for DUSP16 as a regulator of JNK signaling was further demonstrated via overexpression in Ba/F3 cells, which increased their antiapoptosis [4].
 

Analytical, diagnostic and therapeutic context of DUSP16

  • Co-immunoprecipitation experiments and histological analysis suggested that MKP-7 determines the localization of MAPKs in the cytoplasm [5].

References

  1. Dynamic interaction between the dual specificity phosphatase MKP7 and the JNK3 scaffold protein beta-arrestin 2. Willoughby, E.A., Collins, M.K. J. Biol. Chem. (2005) [Pubmed]
  2. Phosphorylation of Ser-446 determines stability of MKP-7. Katagiri, C., Masuda, K., Urano, T., Yamashita, K., Araki, Y., Kikuchi, K., Shima, H. J. Biol. Chem. (2005) [Pubmed]
  3. Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446. Masuda, K., Shima, H., Katagiri, C., Kikuchi, K. J. Biol. Chem. (2003) [Pubmed]
  4. MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome region 12p12-13, reduces BCR-ABL-induced transformation. Hoornaert, I., Marynen, P., Goris, J., Sciot, R., Baens, M. Oncogene (2003) [Pubmed]
  5. MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein. Masuda, K., Shima, H., Watanabe, M., Kikuchi, K. J. Biol. Chem. (2001) [Pubmed]
  6. A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs. Tanoue, T., Yamamoto, T., Maeda, R., Nishida, E. J. Biol. Chem. (2001) [Pubmed]
 
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