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研究生:陳威仁
研究生(外文):Chen, Wei-Ren
論文名稱:PAK自我磷酸化依賴性蛋白質激活脢之調節性自我磷酸化作用點分析其屬於家族一員的証據
論文名稱(外文):Identification of the Regulatory Autophosphorylation Site of Autophosphorylation-Dependent Protein Kinase(Auto-kinase), Evidence that Auto-kinase Belongs to a Member of PAK Family
指導教授:余兆松楊孝德黃銓珍
指導教授(外文):Yu, Zhao-SongYang, Xiao-DeHuang, Quan-Zhen
學位類別:碩士
校院名稱:長庚大學
系所名稱:基礎醫學研究所
學門:醫藥衛生學門
學類:醫學學類
論文種類:學術論文
論文出版年:1997
畢業學年度:85
語文別:中文
論文頁數:84
中文關鍵詞:自我磷酸化依賴性蛋白質激活脢醫學基礎醫學
外文關鍵詞:Autophosphorylation-dependent protein kinaseMEDICINEPRECLINICAL-SCIENCE
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Autophosphorylation-dependent protein kinase(auto-kinase)
was found existing in pig brain and liver in 1987 by Yang et al.
with a unique property that its activity is regulated by
autophosphorylation.Auto-kinase is a cyclic nucleotide- and
calcium-independent protein kinase, and its molecular weight is
36kDa. Subsequent studies revealed that auto-kinase is a
multisubstrate protein kinase which can act on several key
regulatory proteins and enzymes with the following substrate
consensus sequence motif:R-X-(X)-S*/T*-X3-S/T (where * is the
kinase target site). However, the gene of auto-kinase has not
yet been cloned and therefore, the founding of auto-kinase as a
new protein kinase is still controversial. Furthermore, the
autophosphorylation site(s) of auto-kinase, which play(s) a
critical role in regulating its activity, has(have) not yet been
identified. To elucidate these points, we purified auto-kinase
was subjected to N-terminal and internal partial sequencing.
Three segments of partial amino acid sequence of auto-kinase
(VDGGAKTSDKQKKKAXMTDE, EKLRTIV and LQNPEI/KLTP/FI) were
successfully obtained. These sequences were perfectly matched
with those of a protein kinase named gamma-p21-Cdc42/Rac-
activated kinase(PAK2), which was identified from human placenta
cDNA library by Martin et al. in 1995, when mapped data bank.
This, together with our finding that auto-kinase can be
specifically recognized by an anti-peptide antibody raised
against the 14-amino acid C-terminal peptide of human PAK2
demonstrated that auto-kinase is a pig homologue of human PAK2.
A synthetic peptide EQSKRSTMVGTPYWMAPEVVTRK (STM peptide)
corresponding to amino acid residue 397-419 of human PAK2, which
possesses the substrate consensus sequence motif for auto-
kinase, can be efficiently phosphorylated by auto-kinase at
threonine residue. Moreover, the tryptic phosphopeptide map of
32P-STM peptide phosphorylated by auto-kinase is identical to
that of 32P-autophosphorylated tryptic phosphopeptides by manual
Edman degradation. These results demonstrated that Thr403
(EQSKRSTMVGTPYWMAPEVVTRK, * indicates the phosphorylation site,
according to the sequence of human PAK2) is the only
autophosphorylation site of auto-kinase.

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