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Structures, Organization, and Function of Reflectin Proteins in Dynamically Tunable Reflective Cells.
DeMartini, Daniel G; Izumi, Michi; Weaver, Aaron T; Pandolfi, Erica; Morse, Daniel E.
Afiliação
  • DeMartini DG; From the Biomolecular Science and Engineering Program, University of California, Santa Barbara, California 93106-9611, the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100, and.
  • Izumi M; the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100, and.
  • Weaver AT; the Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, California 93106-9610.
  • Pandolfi E; the Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, California 93106-9610.
  • Morse DE; From the Biomolecular Science and Engineering Program, University of California, Santa Barbara, California 93106-9611, the Institute for Collaborative Biotechnologies, University of California, Santa Barbara, California 93106-5100, and the Department of Molecular, Cellular and Developmental Biology,
J Biol Chem ; 290(24): 15238-49, 2015 Jun 12.
Article em En | MEDLINE | ID: mdl-25918159
ABSTRACT
The reversible assembly of reflectin proteins drives dynamic iridescence in cephalopods. Squid dynamically tune the intensity and colors of iridescence generated by constructive interference from intracellular Bragg reflectors in specialized skin cells called iridocytes. Analysis of the tissue specificity of reflectin subtypes reveals that tunability is correlated with the presence of one specific reflectin sequence. Differential phosphorylation and dephosphorylation of the reflectins in response to activation by acetylcholine, as well as differences in their tissue-specific and subcellular spatial distributions, further support the suggestion of different roles for the different reflectin subtypes.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Limite: Animals Idioma: En Revista: J Biol Chem Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Limite: Animals Idioma: En Revista: J Biol Chem Ano de publicação: 2015 Tipo de documento: Article