TY - JOUR
T1 - The human IFN-inducible p53 target gene TRIM22 colocalizes with the centrosome independently of cell cycle phase.
AU - Petersson, Jessica
AU - Lönnbro, Per
AU - Herr, Anna-Maria
AU - Mörgelin, Matthias
AU - Gullberg, Urban
AU - Drott, Kristina
PY - 2010
Y1 - 2010
N2 - TRIM22 (Staf50), a member of the TRIM protein family, is an interferon (IFN)-inducible protein as well as a p53 target gene. The function of TRIM22 is largely unknown, but TRIM22 is suggested to play a role in viral defense by restriction of viral replication. In addition, TRIM22 may function as a ubiquitin E3 ligase. In contrast to previous reports showing solely cytoplasmic localization of exogenous TRIM22, we report here that endogenous TRIM22 is localized to both nucleus and cytosol in primary human mononuclear cells, as well as in the human osteosarcoma cell line U2OS. Moreover, we demonstrate a colocalization of TRIM22 with the centrosomes in primary cells as well as in U2OS cells, and show that this colocalization is independent of cell cycle phase. Additionally, our data suggest the colocalization with centrosomes to be independent on the microtubule network. Given that some viral protein assembly takes place in the close vicinity of the centrosome, our data suggest that important functions of TRIM22 such as regulation of viral replication and protein degradation may take place in the centrosome. However, further studies are warranted to certify this notion.
AB - TRIM22 (Staf50), a member of the TRIM protein family, is an interferon (IFN)-inducible protein as well as a p53 target gene. The function of TRIM22 is largely unknown, but TRIM22 is suggested to play a role in viral defense by restriction of viral replication. In addition, TRIM22 may function as a ubiquitin E3 ligase. In contrast to previous reports showing solely cytoplasmic localization of exogenous TRIM22, we report here that endogenous TRIM22 is localized to both nucleus and cytosol in primary human mononuclear cells, as well as in the human osteosarcoma cell line U2OS. Moreover, we demonstrate a colocalization of TRIM22 with the centrosomes in primary cells as well as in U2OS cells, and show that this colocalization is independent of cell cycle phase. Additionally, our data suggest the colocalization with centrosomes to be independent on the microtubule network. Given that some viral protein assembly takes place in the close vicinity of the centrosome, our data suggest that important functions of TRIM22 such as regulation of viral replication and protein degradation may take place in the centrosome. However, further studies are warranted to certify this notion.
U2 - 10.1016/j.yexcr.2009.12.007
DO - 10.1016/j.yexcr.2009.12.007
M3 - Article
C2 - 20006605
SN - 1090-2422
VL - 316
SP - 568
EP - 579
JO - Experimental Cell Research
JF - Experimental Cell Research
ER -