Abstract：
:Akt activation has been implicated broadly in tumorigenesis, but the basis for its dysregulation in cancer cells is incompletely understood. In this study, we sought to clarify a regulatory role for the Akt-binding carboxy-terminal modulator protein (CTMP), which has been controversial. In evaluating CTMP expression in paired normal-tumor specimens of 198 patients with breast cancer, we found that CTMP was upregulated in breast tumors, where it was associated with poor patient survival. Notably, CTMP expression also correlated positively with Akt phosphorylation in breast cancer clinical specimens and cell lines. Furthermore, ectopic expression of CTMP promoted cell proliferation and enhanced the tumorigenic properties of estrogen-dependent breast cancer cells. This effect was correlated with increased sensitivity to insulin-induced Akt phosphorylation, which is mediated primarily by the phosphoinositide 3-kinase-Akt pathway. In contrast, short hairpin RNA-mediated silencing of endogenous CTMP decreased the proliferation of estrogen-dependent or estrogen-independent breast cancer cells. Mechanistic investigations defined the N-terminal domain of CTMP at amino acids 1 to 64 as responsible for Akt binding. Taken together, our results firmly corroborate the concept that CTMP promotes Akt phosphorylation and functions as an oncogenic molecule in breast cancer.
journal_name
Cancer Resjournal_title
Cancer researchauthors
Liu YP,Liao WC,Ger LP,Chen JC,Hsu TI,Lee YC,Chang HT,Chen YC,Jan YH,Lee KH,Zeng YH,Hsiao M,Lu PJdoi
10.1158/0008-5472.CAN-13-0518subject
Has Abstractpub_date
2013-10-15 00:00:00pages
6194-205issue
20eissn
0008-5472issn
1538-7445pii
0008-5472.CAN-13-0518journal_volume
73pub_type
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