Dimerization of TRAF-interacting protein (TRAIP) regulates the mitotic progression.

Biochem Biophys Res Commun

Department of Biological Sciences, Sungkyunkwan University (SKKU), Suwon 440-746, Republic of Korea. Electronic address:

Published: August 2015

AI Article Synopsis

  • The TRAF-interacting protein (TRAIP) plays a significant role in early mitotic progression and ensuring proper chromosome alignment during metaphase.
  • TRAIP is a 469 amino acid protein that contains critical structural domains including RING, coiled-coil (CC), and leucine zipper (LZ) which facilitate its homo- or hetero-dimerization.
  • Research using TRAIP mutants revealed that the CC domain is essential for TRAIP's homo-dimerization; cells lacking this domain showed increased mitotic index and enhanced progression through mitosis.

Article Abstract

The homo- or hetero-dimerization of proteins plays critical roles in the mitotic progression. The TRAF-interacting protein (TRAIP) is crucial in early mitotic progression and chromosome alignment defects in the metaphase. The TRAIP is a 469 amino acid protein, including the Really Interesting New Gene (RING), coiled-coil (CC), and leucine zipper (LZ) domain. In general, the CC or LZ domain containing proteins forms homo- or hetero-dimerization to achieve its activity. In this study, a number of TRAIP mutants were used to define the TRAIP molecular domains responsible for its homo-dimerization. A co-immunoprecipitation assay indicated that the TRAIP forms homo-dimerization through the CC domain. The cells, expressing the CC domain-deleted mutant that could not form a homo-dimer, increased the mitotic index and promoted mitotic progression.

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http://dx.doi.org/10.1016/j.bbrc.2015.06.026DOI Listing

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