| Summary: | 碩士 === 長庚大學 === 基礎醫學研究所 === 93 === p21-activated kinase (PAKs) belong to a family of Serine/Threonine kinase activated by small G proteins. γ-PAK (PAK2) one of the group I PAKs has been studied widely and shown to be involved in the regulation of apoptosis, cell morphology, cell motility, actin reorganization and transformation. To identify possible regulators of PAK2, a proteomic approach was employed to find the PAK2-interacting proteins. Endogenous PAK2 and its interaction proteins were immunopreciptated with a polyclonal anti-PAK2 (N17) antibody. After separated with 8% SDS-PAGE and silver staining, several candidates of PAK2-interacting proteins were observed and their identities were examined by MALDI-TOF mass spectrometry. Among them, a protein band near 200 kDa was identified as PDZ-containing Myosin (MysPDZ). The aim of this thesis is to confirm the interaction between MysPDZ and PAK2-interacting protein complexes, and to investigate the role of MysPDZ in PAK2 signaling pathway. Using different MysPDZ deletion mutants, I demonstrated that the amino acid 1768~2054 of MysPDZ was responsible for its interaction with the PAK2-interacting protein complexes, and the amino acid 1768~1971 and 1971~2054 (the region between coiled-coil domain and non coiled-coil domain) in the C-terminal portion of MysPDZ is critical for this molecule to participate in the PAK2-interacting protein complexes. Further investigation will be focused on the biological significance of this interaction.
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