CEP55 Protein Overview: Sequence, Structure, Function and Protein Interaction

CEP55 Protein Overview

Fabbro et al. (2005) found that association of CEP55 with centrioles was independent of microtubules and was not required for microtubule nucleation. Upon mitotic entry, phosphorylation of CEP55 at ser425 and ser428 by ERK2 (MAPK1; 176948) and CDK1 (CDC2; 116940) triggered dissociation of CEP55 from centrosomes. This phosphorylation enhanced binding of PLK1 (602098) to CEP55, leading to phosphorylation of CEP55 at ser436. Phosphorylated CEP55 localized to the midbody. Expression of a phosphorylation-deficient CEP55 mutant or deletion of CEP55 by small interfering RNA resulted in failure of mitotic exit and cytokinesis. By immunoprecipitating epitope-tagged human CEP55 expressed by transfected Chinese hamster ovary cells, Martinez-Garay et al. (2006) found that CEP55 could form homodimers. By immunohistochemical analysis, Chen et al. (2007) showed that expression of CEP55 was upregulated in liver cancer tissue compared with adjacent normal tissue. Patients with higher CEP55 expression had a poorer survival than those with lower expression. CEP55 promoted anchorage-independent growth, enhanced cell growth at low serum levels, and induced tumorigenesis in nude mice. CEP55-elicited cell transformation was mediated by activation of the PI3K (see 601232)/AKT (see 164730) pathway. Moreover, CEP55 formed a complex with PI3K and activated PI3K activity. Using RT-PCR, Chen et al. (2009) detected overexpression of CEP55 in oral cavity squamous cell carcinoma (OCSCC). High CEP55 expression correlated with advanced tumor node metastasis stage and reduced 5-year survival rate. CEP55 stimulated cell migration and invasion by increasing expression of FOXM1 (602341) and MMP2 (120360). Immunohistochemical and Western blot analyses of aggressive OCSCCs confirmed a positive correlation between expression of CEP55 and that of FOXM1 and MMP2. Iwamori et al. (2010) stated that cytokinesis is initiated by MKLP1 (KIF23; 605064)-mediated recruitment of CEP55, followed by CEP55-mediated recruitment of ALIX (PDCD6IP; 608074) and TSG101 (601387). Using protein pull-down experiments, Iwamori et al. (2010) showed that mouse Tex14 interacted with Cep55 in transfected HEK293T cells. Mutation analysis revealed that the GPPX3Y motif of mouse and human TEX14 interacted with the central hinge region of CEP55. Interaction of TEX14 with CEP55 blocked the interaction of CEP55 with ALIX and TSG101, although TEX14 did not itself interact significantly with ALIX or TSG101. Overexpression of TEX14 in HeLa cells blocked endogenous ALIX and TSG101 from interacting with CEP55, preventing abscission and resulting in stabilization of transient intercellular bridges. Iwamori et al. (2010) concluded that formation of intercellular bridges in germ cells involves preferential interaction of CEP55 with TEX14 rather than ALIX and TSG101, leading to formation of stable intercellular bridges and delayed abscission.

CEP55 protein name

Recommended name
Centrosomal protein of 55 kDa
Aliases
cancer / testis antigen 111, CT111, FLJ10540

CEP55 Protein Molecular Weight & PI

The parameters have been computed for the following feature

FT CHAIN 1-464 Centrosomal protein of 55 kDa.

Molecular weight (Da)

54178.24

Theoretical pI

6.55

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