Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/78531
Title: MOLECULAR CHARACTERIZATION OF THE POST-TRANSLATIONAL REGULATORY MECHANISM OF MOAP-1
Authors: BAY WAN PING
Keywords: apoptosis, MOAP-1, Bax-binding partner, ubiquitination, phosphorylation
Issue Date: 20-Jan-2014
Citation: BAY WAN PING (2014-01-20). MOLECULAR CHARACTERIZATION OF THE POST-TRANSLATIONAL REGULATORY MECHANISM OF MOAP-1. ScholarBank@NUS Repository.
Abstract: Bcl-2 protein family regulates the commitment of cells to apoptosis. By regulating the activation of Bax and Bak, these proteins control the release of apoptogenic factors from mitochondria. MOAP-1 was cloned as a Bax-associating protein. In healthy cells, MOAP-1 is a short-lived protein, which is constitutively degraded. Apoptotic stimuli stabilize MOAP-1 and induce its association with Bax. Higher levels of MOAP-1 sensitize cancer cells to chemotherapeutic drugs, suggesting mechanisms that are involved in regulating its protein stability can be valuable targets for cancer treatment. Understanding of the post-translational modifications of MOAP-1 is vital. In this study, we examined ubiquitination and phosphorylation as prospective regulatory mechanisms of MOAP-1. We identified TRIM11 as a putative E3 ubiquitin ligase of MOAP-1 and revealed that protein stability of MOAP-1 is regulated by phosphorylation at serines 27, 29 and 31 and demonstrated the involvement of the ERK/MAPK signaling in regulation of MOAP-1.
URI: http://scholarbank.nus.edu.sg/handle/10635/78531
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