Y
Yuichi Takakuwa
Researcher at Tufts University
Publications - 62
Citations - 2856
Yuichi Takakuwa is an academic researcher from Tufts University. The author has contributed to research in topics: Calmodulin & Membrane protein. The author has an hindex of 26, co-authored 62 publications receiving 2709 citations.
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The FERM domain: A unique module involved in the linkage of cytoplasmic proteins to the membrane
Athar H. Chishti,Anthony C. Kim,Shirin M. Marfatia,Mohini Lutchman,Manjit Hanspal,Hitesh K. Jindal,Shih Chun Liu,Philip S. Low,Guy A. Rouleau,Narla Mohandas,Joel Anne Chasis,John G. Conboy,Phillipe Gascard,Yuichi Takakuwa,Shu-Ching Huang,Edward J. Benz,Anthony Bretscher,Richard G. Fehon,James F. Gusella,Vijaya Ramesh,Frank Solomon,Vincent T. Marchesi,Shoichiro Tsukita,Sachiko Tsukita,Monique Arpin,Daniel Louvard,Nicholas K. Tonks,James M. Anderson,Alan S. Fanning,Peter J. Bryant,Daniel F. Woods,Kevin B. Hoover +31 more
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Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability
TL;DR: It is documented that maintenance of asymmetric distribution of phospholipids resulted in improved membrane mechanical stability and enabled a functional role of lipid asymmetry in regulating membrane material properties to be documented.
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Modulation of Erythrocyte Membrane Mechanical Function by Protein 4.1 Phosphorylation
TL;DR: It is shown that the phosphorylation of 4.1R by PKC results in its decreased ability to form a ternary complex with spectrin and actin as well as dissociation of glycophorin C from the membrane skeleton, and a marked decrease in membrane mechanical stability.
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Molecular and Functional Characterization of Protein 4.1B, a Novel Member of the Protein 4.1 Family with High Level, Focal Expression in Brain
Marilyn Parra,Philippe Gascard,Loren D. Walensky,J. Aura Gimm,Seth Blackshaw,Nadine Chan,Yuichi Takakuwa,Trish Berger,Gloria Lee,Joel Anne Chasis,Solomon H. Snyder,Narla Mohandas,John G. Conboy +12 more
TL;DR: Results indicate that 4.1B transcription is selectively regulated among neuronal populations and that alternative splicing regulates expression of 4.2B isoforms possessing critical functional domains typical of other protein 4.
Journal ArticleDOI
Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction.
Wataru Nunomura,Yuichi Takakuwa,Reiko Tokimitsu,Sharon Wald Krauss,Makoto Kawashima,Narla Mohandas +5 more
TL;DR: It is reported here that protein 4.1 binds to the cytoplasmic domain of CD44 with a dissociation constant on the order of 10−7 m and that Ca2+ and calmodulin reduce the affinity of this interaction.