The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

NUMA1  -  nuclear mitotic apparatus protein 1

Homo sapiens

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of NUMA1

 

Psychiatry related information on NUMA1

  • We tested this prediction in the mammalian mitotic extract and, consistent with the model, found that increasing the contribution of microtubule cross-linking by NuMA compensated for the loss of Eg5 motor activity [5].
 

High impact information on NUMA1

 

Chemical compound and disease context of NUMA1

 

Biological context of NUMA1

 

Anatomical context of NUMA1

 

Associations of NUMA1 with chemical compounds

 

Physical interactions of NUMA1

 

Regulatory relationships of NUMA1

 

Other interactions of NUMA1

  • We also found that 4.1G, a ubiquitous homolog of 4.1R, is present in mutated as well as control cells and that its C-terminal region binds efficiently to NuMA, suggesting that in fact mitotic spindles host a mixture of the two 4.1 family members [21].
  • Mammalian Pins is a conformational switch that links NuMA to heterotrimeric G proteins [6].
  • NuMA transport is required for spindle pole assembly and maintenance, since disruption of the dynactin complex (by increasing the amount of the dynamitin subunit) or dynein function (with an antibody) strongly inhibits NuMA translocation and accumulation and disrupts spindle pole assembly [15].
  • Overexpression of the C-terminal tail of Lgl2 induced mis-localization of the nuclear mitotic apparatus protein NuMA and disorganization of the mitotic spindle during mitosis, eventually causing formation of multiple micronuclei [22].
  • In contrast, cases with t(11;17)(q13;q21) and t(5;17)(q35;q21) which fuse RARA with NuMA and NPM, respectively, were reported to be sensitive to ATRA [23].
 

Analytical, diagnostic and therapeutic context of NUMA1

References

  1. Myeloid leukemia with promyelocytic features in transgenic mice expressing hCG-NuMA-RARalpha. Sukhai, M.A., Wu, X., Xuan, Y., Zhang, T., Reis, P.P., Dubé, K., Rego, E.M., Bhaumik, M., Bailey, D.J., Wells, R.A., Kamel-Reid, S., Pandolfi, P.P. Oncogene (2004) [Pubmed]
  2. Association of the NuMA region on chromosome 11q13 with breast cancer susceptibility. Kammerer, S., Roth, R.B., Hoyal, C.R., Reneland, R., Marnellos, G., Kiechle, M., Schwarz-Boeger, U., Griffiths, L.R., Ebner, F., Rehbock, J., Cantor, C.R., Nelson, M.R., Braun, A. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  3. Nuclear proteins of the bovine esophageal epithelium. II. The NuMA gene gives rise to multiple mRNAs and gene products reactive with monoclonal antibody W1. Tang, T.K., Tang, C.J., Chen, Y.L., Wu, C.W. J. Cell. Sci. (1993) [Pubmed]
  4. NuMA and nuclear lamins are cleaved during viral infection--inhibition of caspase activity prevents cleavage and rescues HeLa cells from measles virus-induced but not from rhinovirus 1B-induced cell death. Taimen, P., Berghäll, H., Vainionpää, R., Kallajoki, M. Virology (2004) [Pubmed]
  5. A mechanistic model for the organization of microtubule asters by motor and non-motor proteins in a mammalian mitotic extract. Chakravarty, A., Howard, L., Compton, D.A. Mol. Biol. Cell (2004) [Pubmed]
  6. Mammalian Pins is a conformational switch that links NuMA to heterotrimeric G proteins. Du, Q., Macara, I.G. Cell (2004) [Pubmed]
  7. Fusion of retinoic acid receptor alpha to NuMA, the nuclear mitotic apparatus protein, by a variant translocation in acute promyelocytic leukaemia. Wells, R.A., Catzavelos, C., Kamel-Reid, S. Nat. Genet. (1997) [Pubmed]
  8. Human-specific nuclear protein that associates with the polar region of the mitotic apparatus: distribution in a human/hamster hybrid cell. Lydersen, B.K., Pettijohn, D.E. Cell (1980) [Pubmed]
  9. Preferential expression of NuMA in the nuclei of proliferating cells. Taimen, P., Viljamaa, M., Kallajoki, M. Exp. Cell Res. (2000) [Pubmed]
  10. A mammalian Partner of inscuteable binds NuMA and regulates mitotic spindle organization. Du, Q., Stukenberg, P.T., Macara, I.G. Nat. Cell Biol. (2001) [Pubmed]
  11. A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein. Mattagajasingh, S.N., Huang, S.C., Hartenstein, J.S., Snyder, M., Marchesi, V.T., Benz, E.J. J. Cell Biol. (1999) [Pubmed]
  12. NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis. Chang, W., Dynek, J.N., Smith, S. Biochem. J. (2005) [Pubmed]
  13. A potential role for human cohesin in mitotic spindle aster assembly. Gregson, H.C., Schmiesing, J.A., Kim, J.S., Kobayashi, T., Zhou, S., Yokomori, K. J. Biol. Chem. (2001) [Pubmed]
  14. Multiple mechanisms regulate NuMA dynamics at spindle poles. Kisurina-Evgenieva, O., Mack, G., Du, Q., Macara, I., Khodjakov, A., Compton, D.A. J. Cell. Sci. (2004) [Pubmed]
  15. Formation of spindle poles by dynein/dynactin-dependent transport of NuMA. Merdes, A., Heald, R., Samejima, K., Earnshaw, W.C., Cleveland, D.W. J. Cell Biol. (2000) [Pubmed]
  16. Tissue phenotype depends on reciprocal interactions between the extracellular matrix and the structural organization of the nucleus. Lelièvre, S.A., Weaver, V.M., Nickerson, J.A., Larabell, C.A., Bhaumik, A., Petersen, O.W., Bissell, M.J. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  17. Dynamic changes of NuMA during the cell cycle and possible appearance of a truncated form of NuMA during apoptosis. Hsu, H.L., Yeh, N.H. J. Cell. Sci. (1996) [Pubmed]
  18. Mutation of the predicted p34cdc2 phosphorylation sites in NuMA impair the assembly of the mitotic spindle and block mitosis. Compton, D.A., Luo, C. J. Cell. Sci. (1995) [Pubmed]
  19. Microinjection of a monoclonal antibody against SPN antigen, now identified by peptide sequences as the NuMA protein, induces micronuclei in PtK2 cells. Kallajoki, M., Harborth, J., Weber, K., Osborn, M. J. Cell. Sci. (1993) [Pubmed]
  20. Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor. Ye, K., Compton, D.A., Lai, M.M., Walensky, L.D., Snyder, S.H. J. Neurosci. (1999) [Pubmed]
  21. A splicing alteration of 4.1R pre-mRNA generates 2 protein isoforms with distinct assembly to spindle poles in mitotic cells. Delhommeau, F., Vasseur-Godbillon, C., Leclerc, P., Schischmanoff, P.O., Croisille, L., Rince, P., Morinière, M., Benz, E.J., Tchernia, G., Tamagnini, G., Ribeiro, L., Delaunay, J., Baklouti, F. Blood (2002) [Pubmed]
  22. Direct binding of Lgl2 to LGN during mitosis and its requirement for normal cell division. Yasumi, M., Sakisaka, T., Hoshino, T., Kimura, T., Sakamoto, Y., Yamanaka, T., Ohno, S., Takai, Y. J. Biol. Chem. (2005) [Pubmed]
  23. Atypical response to all-trans retinoic acid in a der(5)t(5;17) acute promyelocytic leukemia. Mozziconacci, M.J., Liberatore, C., Grignani, F., Sainty, D., Pelicci, P.G., Birg, F., Lafage-Pochitaloff, M. Leukemia (1999) [Pubmed]
  24. GAS41, a highly conserved protein in eukaryotic nuclei, binds to NuMA. Harborth, J., Weber, K., Osborn, M. J. Biol. Chem. (2000) [Pubmed]
  25. Overexpression of normal and mutant Arp1alpha (centractin) differentially affects microtubule organization during mitosis and interphase. Clark, I.B., Meyer, D.I. J. Cell. Sci. (1999) [Pubmed]
 
WikiGenes - Universities