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Human PCID2 plays analogous roles to Centrin 2 outside of the TREX‐2 complex.
Author(s) -
Cunningham Corey Nathaniel,
Schmidt Casey Alexandra,
Resendes Karen Kay
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.767.1
Subject(s) - centrosome , microbiology and biotechnology , nuclear transport , gene knockdown , nuclear export signal , nucleoporin , nuclear pore , biology , chemistry , cell cycle , cell nucleus , cell , gene , nucleus , genetics
Human PCID2, is characterized by its PCI interaction domain and its involvement in the mammalian transcription export complex, TREX‐2. One component of the TREX‐2 complex, Centrin‐2, is known to be involved in protein export in addition to mRNA export and was originally identified as a component of the centrosome. We attempted to determine if PCID2 also performs these other functions in the cell. We have demonstrated that PCID2 colocalizes with γ‐tubulin and centrin‐2 at the centrosome of HeLa cells. Furthermore, knockdown of PCID2, while not affecting nuclear protein import, does lead to a delay in nuclear protein export. In contrast we have demonstrated that another TREX‐2 component, Eny2, is not present at the centrosome nor is it involved in nuclear protein transport. Therefore, our results indicate that PCID2 distinctly serves roles outside of the TREX‐2 complex that parallel the function of Centrin‐2.