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Regulation of bifunctional proteins in cells: Lessons from the phospholipase Cβ/G protein pathway
Author(s) -
Jackson Lela,
Qifti Androniqi,
Pearce Katherine M.,
Scarlata Suzanne
Publication year - 2020
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3809
Subject(s) - microbiology and biotechnology , phospholipase , translation (biology) , function (biology) , phospholipase c , calcium signaling , bifunctional , chemistry , biology , intracellular , biochemistry , enzyme , signal transduction , messenger rna , gene , catalysis
Some proteins can serve multiple functions depending on different cellular conditions. An example of a bifunctional protein is inositide‐specific mammalian phospholipase Cβ (PLCβ). PLCβ is activated by G proteins in response to hormones and neurotransmitters to increase intracellular calcium. Recently, alternate cellular function(s) of PLCβ have become uncovered. However, the conditions that allow these different functions to be operative are unclear. Like many mammalian proteins, PLCβ has a conserved catalytic core along with several regulatory domains. These domains modulate the intensity and duration of calcium signals in response to external sensory information, and allow this enzyme to inhibit protein translation in a noncatalytic manner. In this review, we first describe PLCβ's cellular functions and regulation of the switching between these functions, and then discuss the thermodynamic considerations that offer insight into how cells manage multiple and competitive associations allowing them to rapidly shift between functional states.

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