2001 Fiscal Year Final Research Report Summary
Functional analysis of a novel intracellular calcium-binding protein peflin
| Project/Area Number |
11460038
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | Nagoya University |
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Principal Investigator |
MAKI Masatoshi Nagoya University, Graduate School of Bioagricultural Sciences, Professor, 大学院・生命農学研究科, 教授 (40183610)
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| Co-Investigator(Kenkyū-buntansha) |
SHIBATA Hideki Nagoya University, Graduate School of Bioagricultural Sciences, Assistant Professor, 大学院・生命農学研究科, 助手 (30314470)
HITOMI Kiyotaka Nagoya University, Graduate School of Bioagricultural Sciences, Associate Professor, 大学院・生命農学研究科, 助教授 (00202276)
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| Project Period (FY) |
1999 – 2001
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| Keywords | peflin / ALG-2 / calcium / EF-hand / interaction / Alix / annexin / dimer |
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| Research Abstract |
Peflin is a new member of the penta-EF-hand (PEF) calcium-binding protein family that includes ALG-2 (apoptosis linked gene 2), calpain, and sorcin. We prepared a specific monoclonal antibody that recognized peflin. By immunoprecipitation followed by Western blot analysis, peflin and ALG-2 have been found to form a heterodimer that dissociates in a calcium-dependent manner. While peflin is localized to cytoplasm, ALG-2 is localized in both cytoplasm and nuclei. Peflin may regulate function of ALG-2 by heterodimerization. We identified PEF proteins in the cellular slime mold Dictyostelium discoideum, a model organism that displays transformation from unicellular form to multicellular form during its life cycle. Phylogenetic analysis has revealed that ALG-2 and/or peflin are conserved and present ubiquitously in higher and lower eukaryotes while calpain and sorcin are rather new in evolution. By the yeast two-hybrid screening, ALG-2, peflin, Alix and annexin XI were isolated as ALG-2-interacting proteins. The N-terminal Gly/Tyr/Pro-rich region of annexin has a sequence similar to that of the C-terminal region of Alix, suggesting presence of a common binding motif in these regions
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