Protein kinase C

By A. Newton. IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology, 2008

901 citations recorded by the source corpus.

Phosphorylation is a universal language used by cells to relay information between and within cells. One family of kinases that plays a key role in transducing information is the protein kinase C family. Members of this family interpret information from signals that result in phospholipid hydrolysis; they communicate to substrates throughout the cell, causing both short-term and long-term changes in cell function. This chapter focuses on the molecular mechanisms of protein kinase C, from the protein to the cell biological level.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/eb17054ed72741f376913f8a135e8957793c3c9e

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Citations in the corpus

• Calcium-dependent PKC isoforms have specialized roles in short-term synaptic plasticity (2014, positive): “…in postnatal day 11– 14 (P11–P14) animals, PTP is mediated primarily by PKCb (Fioravante et al., 2011), one of the ''classical'' calcium-dependent isoforms (PKCa, PKCb, and PKCg), as opposed to the many calcium-insensitive ''novel'' and ''atypical'' isoforms (Newton, 1995, 2001; Steinberg, 2008).”
• Cell and Molecular Biology (2009, background): “The conventional PKC isoforms (cPKCs: a, b, and g isoforms) depend on calcium and diacylglycerol (DAG) for activation; the novel PKC isoforms (nPKCs: d, e, , and y) only depend on DAG, whereas the atypical PKC isoforms (aPKCs: l and x) are activated independent of calcium and DAG (Newton, 2001).”