A CH domain-containing N terminus in NuMA?
Nuclear mitotic apparatus protein (NuMA) is an essential vertebrate component in organizing microtubule ends at spindle poles. The NuMA-dynactin/dynein motor multiprotein complex not only explains the transport of NuMA along spindle fibers but also is linked to the process of microtubule focusing. The interaction sites of NuMA to dynein/dynactin have not been mapped. In the yet functionally uncharacterized N terminus of NuMA, we predict a calponin-homology (CH) domain, a motif with binding activity for actin-like molecules. We substantiate the primary sequence analysis-based prediction with secondary structure and fold recognition analysis, and we propose the N-terminal CH domain of NuMA as a likely interaction site for actin-related protein 1 (Arp1) protein of the dynactin/dynein complex.
Novatchkova
Maria
M
Research Institute of Molecular Pathology, A-1030 Vienna, Austria.
Eisenhaber
Frank
F
D000595:Amino Acid Sequence; D034961:Antigens, Nuclear; D002135:Calcium-Binding Proteins / Q000737:chemistry; D018797:Cell Cycle Proteins; D006801:Humans; D008840:Microfilament Proteins; D008969:Molecular Sequence Data; D034521:Nuclear Matrix-Associated Proteins; D009687:Nuclear Proteins / Q000737:chemistry* / Q000502:physiology; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D000096985:Calponins
D034961:Antigens, Nuclear; D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; D008840:Microfilament Proteins; D034521:Nuclear Matrix-Associated Proteins; D009687:Nuclear Proteins; D000096985:Calponins; C050045:NUMA1 protein, human