|
|
|
|
|
|
|
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
Journal of Cell Science, Vol 104, Issue 2 249-260, Copyright © 1993 by Company of Biologists
JOURNAL ARTICLES |
TK Tang, CJ Tang, YL Chen and CW Wu
Laboratory of Cell Biology, Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.
Treatment of small cells derived from the basal layer of bovine esophageal epithelium, with Triton X-100, urea and sonication resulted in a nuclear residue that was used as an immunogen for generation of monoclonal antibodies directed against nuclear components. One such antibody, designated W1, was found to label the nuclei of all cells examined. In interphase cells, the target antigen of antibody W1 was diffusely distributed in the nucleus. During metaphase, however, the W1 antigen formed prominent crescents at the poles of the mitotic spindle, diminished gradually in anaphase, and finally redistributed into the regenerating daughter nuclei. Western blotting with antibody W1 yielded a prominent polypeptide of M(r) approximately 230,000. The amino acid sequence, deduced from the nucleotide sequence of several overlapping cDNA clones that span the entire coding region, revealed that the W1 polypeptide was identical to the Nuclear Mitotic Apparatus (NuMA) protein, with a long alpha-helical central core flanked by two nonhelical domains. Interestingly, most cDNA sequences were identical to each other, except for six sequence blocks which were either inserted or deleted in individual cDNA clones. Analysis of the cDNA sequences of various clones, coupled with polymerase chain reaction amplification of cellular mRNA and genomic Southern blotting with region-specific probes, all indicated that multiple mRNA species were present in U-251 human glioma cells, derived from alternative splicing of the RNA transcript from a single NuMA/W1 gene. Besides the predominant form of the mRNA giving rise to the polypeptide of M(r) approximately 230,000, two other forms of mRNA, which arise as a result of alternative splicing and which use different translation termination codons, may yield lower molecular weight polypeptide products. Consistent with this notion, polypeptides of M(r) approximately 195,000 and approximately 194,000 have been observed in this and other studies on the NuMA/W1 protein. These data suggest that multiple isoforms of the NuMA polypeptides generated by alternative mRNA splicing may play some important functions which remain to be characterized.
This article has been cited by other articles:
|
|
 |
|
  P. C. Abad, J. Lewis, I. S. Mian, D. W. Knowles, J. Sturgis, S. Badve, J. Xie, and S. A. Lelievre NuMA Influences Higher Order Chromatin Organization in Human Mammary Epithelium Mol. Biol. Cell, February 1, 2007; 18(2): 348 - 361. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. C. Abad, I. S. Mian, C. Plachot, A. Nelpurackal, C. Bator-Kelly, and S. A. Lelievre The C terminus of the nuclear protein NuMA: Phylogenetic distribution and structure Protein Sci., October 22, 2004; 13(10): 2573 - 2577. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C.-L. Hou, C.-j. C. Tang, S. R. Roffler, and T. K. Tang Protein 4.1R binding to eIF3-p44 suggests an interaction between the cytoskeletal network and the translation apparatus Blood, July 15, 2000; 96(2): 747 - 753. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Melnick and J. D. Licht Deconstructing a Disease: RAR{alpha}, Its Fusion Partners, and Their Roles in the Pathogenesis of Acute Promyelocytic Leukemia Blood, May 15, 1999; 93(10): 3167 - 3215. [Full Text] [PDF]
|
|
|
|
 |
|
 S. N. Mattagajasingh, S.-C. Huang, J. S. Hartenstein, M. Snyder, V. T. Marchesi, and E. J. Benz Jr. A Nonerythroid Isoform of Protein 4.1R Interacts with the Nuclear Mitotic Apparatus (NuMA) Protein J. Cell Biol., April 5, 1999; 145(1): 29 - 43. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A Merdes and D. Cleveland The role of NuMA in the interphase nucleus J. Cell Sci., January 1, 1998; 111(1): 71 - 79. [Abstract] [PDF]
|
|
|
|
|
|
A Saredi, L Howard, and D. Compton Phosphorylation regulates the assembly of NuMA in a mammalian mitotic extract J. Cell Sci., January 6, 1997; 110(11): 1287 - 1297. [Abstract] [PDF]
|
|
|
|
|
|
A. Saredi, L. Howard, and D. A. Compton NuMA assembles into an extensive filamentous structure when expressed in the cell cytoplasm J. Cell Sci., March 1, 1996; 109(3): 619 - 630. [Abstract] [PDF]
|
|
|
|
|
|
H. Hsu and N. Yeh Dynamic changes of NuMA during the cell cycle and possible appearance of a truncated form of NuMA during apoptosis J. Cell Sci., January 2, 1996; 109(2): 277 - 288. [Abstract] [PDF]
|
|
|
|
|
|
C. Sparks, E. Fey, C. Vidair, and S. Doxsey Phosphorylation of NUMA occurs during nuclear breakdown and not mitotic spindle assembly J. Cell Sci., January 11, 1995; 108(11): 3389 - 3396. [Abstract] [PDF]
|
|
|
|
|
|
D. Compton and C Luo Mutation of the predicted p34cdc2 phosphorylation sites in NuMA impair the assembly of the mitotic spindle and block mitosis J. Cell Sci., January 2, 1995; 108(2): 621 - 633. [Abstract] [PDF]
|
|
|
|
|
|
T. Tang, C. Tang, Y. Chao, and C. Wu Nuclear mitotic apparatus protein (NuMA): spindle association, nuclear targeting and differential subcellular localization of various NuMA isoforms J. Cell Sci., January 6, 1994; 107(6): 1389 - 1402. [Abstract] [PDF]
|
|
|
|
|
|
T. Tang, T. Hong, C. Lin, M. Lai, C. Liu, H. Lo, M. Wang, L. Chen, W. Chen, W Ip, et al. Nuclear proteins of the bovine esophageal epithelium. I. Monoclonal antibody W2 specifically reacts with condensed nuclei of differentiated superficial cells J. Cell Sci., January 2, 1993; 104(2): 237 - 247. [Abstract] [PDF]
|
|
|
|
 |
|
 B. Amir-Ahmady and L. M. Salati Regulation of the Processing of Glucose-6-phosphate Dehydrogenase mRNA by Nutritional Status J. Biol. Chem., March 23, 2001; 276(13): 10514 - 10523. [Abstract] [Full Text] [PDF]
|
|
