Identification of the T-complex protein as a binding partner for newly synthesized cytoplasmic dynein intermediate chain 2

Oezdemir A., Machida K., Imataka H., Catling A. D.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, cilt.469, sa.1, ss.126-131, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 469 Sayı: 1
  • Basım Tarihi: 2016
  • Doi Numarası: 10.1016/j.bbrc.2015.11.082
  • Dergi Adı: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.126-131
  • Anahtar Kelimeler: T complex protein 1, CCT, Dynein, Dynein intermediate chain, IC-2, Folding, IN-VIVO, DYNACTIN INTERACTION, MAMMALIAN-CELLS, CHAPERONIN CCT, PHOSPHORYLATION, TRIC/CCT, MITOSIS
  • Gazi Üniversitesi Adresli: Evet

Özet

Cytoplasmic dynein is a macromolecular motor complex with diverse function's in eukaryotic cells. Dynein plays essential roles in intracellular transport of organelles and mitosis, mediated in part by interactions between the dynein intermediate chain 2 (IC-2) subunits and adapter proteins that bind specific cargos. In experiments to identify phosphorylation-dependent binding partners for IC-2 we instead identified a phosphorylation-independent binding partner, the cytosolic chaperonin containing T complex protein 1 (CCT). CCT consists of eight subunits (CCT1-8) and facilitates folding of a subset of newly synthesized proteins. We confirmed interactions between IC-2 and CCT5 and CCT8 in co-immunoprecipitation experiments and determined that the C-terminal half of IC-2 is necessary and sufficient to bind CCT8. Interestingly, co-immunoiprecipitation of IC-2 and CCT is abolished by prior cycloheximide treatment of cells, suggesting that CCT participates in folding of nascent IC-2. In vitro translation experiments employing recombinant CCT complex demonstrated that CCT is able to bind newly synthesized IC-2 after release from the ribosome consistent with a role in folding of IC-2. (C) 2015 Elsevier Inc. All rights reserved.