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Removal of Potential Phosphorylation Sites does not Alter Creatine Transporter Response to PKC or Substrate Availability
Author(s) -
Lucia Santacruz,
Marcus D. Darrabie,
Rajashree Mishra,
Danny O. Jacobs
Publication year - 2015
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000430359
Subject(s) - creatine , phosphocreatine , phosphorylation , creatine kinase , biochemistry , intracellular , transporter , microbiology and biotechnology , biology , kinase , chemistry , endocrinology , gene , energy metabolism
Creatine, Phosphocreatine, and creatine kinases, constitute an energy shuttle that links ATP production in mitochondria with cellular consumption sites. Myocytes and neurons cannot synthesize creatine and depend on uptake across the cell membrane by a specialized transporter to maintain intracellular creatine levels. Although recent studies have improved our understanding of creatine transport in cardiomyocytes, the structural elements underlying the creatine transporter protein regulation and the relevant intracellular signaling processes are unknown.

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