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  • 02월 22일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Mutation of the hydrophobic motif to phosphorylation-deficient mutant renders PKCδ apoptotically more active

등록일
2008년 2월 13일 17시 17분 33초
접수번호
1152
발표코드
31P48포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
Mrigendra B. Karmacharya, 소재원
인하대학교 화학과,
Protein Kinase C (PKC) is a multi-gene subfamily of serine-threonine kinases comprising of at least ten isoforms which play important roles in multitudes of cellular processes as proliferation, differentiation, growth, and apoptosis. PKCδ is one of the important isoforms among the PKCs in regulating various cellular processes including cell survival and apoptosis. Activation of PKCδ is correlated with apoptosis in various cell types. Phosphorylation of Thr505, Ser643 and Ser662 are crucial in activation of PKCδ. Furthermore, phosphorylation of tyrosine residues, in particular that of Tyr311, is related with PKCδ activation and induction of apoptosis. Here, we mutated Ser662 to Ala and generated phosphorylation-deficient mutant of PKCδ (PKCδ-S662A) and studied the effect of this mutation in inducing apoptosis in L929 murine fibroblsasts. We report that this mutation renders PKCδ apoptotically more active. Furthermore, the mutant PKCδ-S662A is more tyrosine phosphorylated and translocated to the membrane faster than its wild type counterpart.

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