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RACK1 was originally isolated and identified as an intracellular protein receptor for protein kinase C, noting the significant homology to the beta subunit of heterotrimeric G proteins. [5] Later studies established RACK1, and its yeast homolog Asc1, as a core ribosomal protein of the eukaryotic small (40S) ribosomal subunit.
Rac1 is a small (~21 kDa) signalling G protein (more specifically a GTPase), and is a member of the Rac subfamily of the family Rho family of GTPases.Members of this superfamily appear to regulate a diverse array of cellular events, including the control of GLUT4 [8] [9] translocation to glucose uptake, cell growth, cytoskeletal reorganization, antimicrobial cytotoxicity, [10] and the ...
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Function. L- glutamate is the major excitatory neurotransmitter in the central nervous system and activates both ionotropic and metabotropic glutamate receptors. Glutamatergic neurotransmission is involved in most aspects of normal brain function and can be perturbed in many neuropathologic conditions. The metabotropic glutamate receptors are a ...
Stress granule formation is often downstream of the stress-activated phosphorylation of eukaryotic translation initiation factor eIF2α; this does not hold true for all types of stressors that induce stress granules, [ 16] for instance, eIF4A inhibition. Further downstream, prion -like aggregation of the protein TIA-1 promotes the formation of ...
A mitogen-activated protein kinase ( MAPK or MAP kinase) is a type of serine/threonine-specific protein kinases involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory cytokines. They regulate cell functions including proliferation, gene expression, differentiation ...
Two 40S ribosomal proteins (RACK1 and RPS6 (or eS6)) have been implicated in cellular signaling: RACK1, first described as the receptor of activated protein kinase C (PKC), is an integral component of the eukaryotic ribosome and is located at the back of the head. [16]
All STAT molecules are phosphorylated by receptor associated kinases, that causes activation, dimerization by forming homo- or heterodimers and finally translocate to nucleus to work as transcription factors. Specifically STAT1 can be activated by several ligands such as Interferon alpha (IFNα), Interferon gamma (IFNγ), Epidermal Growth ...