Receptors for activated C-kinase (RACKs) are scaffold proteins for protein kinase C (PKC). It is composed of seven WD repeats, thus resembling the structure of the β subunit of G proteins. It is not a substrate of PKC, but in its presence, the activity of PKC is increased by several fold.
RACK1 is a receptor for activated C kinases that functions downstream of the growth factor receptor signaling pathway. RACK1 also modulates several functions such as cell adhesion, chemotaxis and protrusion. Increased RACK1 expression has been associated with cell migration and metastasis in breast carcinoma. Thus, RACK1 can be used as a prognostic indicator for breast cancer
Receptors for activated C-kinase (RACKs) anchor activated protein kinase C (PKC) at the site of translocation. RACK1 is the selective RACK for PKCβII. In addition to anchoring activated PKC, RACK1 anchors other signaling enzymes such as sarcoma Src tyrosine kinase, integrin and phosphodiesterase 4D5. The ability of RACK1 to interact simultaneously with different signaling molecules, allows it to integrate inputs from distinct signaling pathways. In mammals, it regulates several processes that involve contact with extracellular matrix such as spreading, the establishment of focal adhesions and cell-cell contacts. Accumulating evidence attributes to it the role of regulating several major nervous system pathways. In addition, RACK1 is a ribosomal protein and a component small subunit and interacts ribosomal RNA. It recruits activated PKC to the ribosome, which in turn, phosphorylates initiation factor 6, leading to ribosome assembly.
物理的形状
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Molecular biology of the cell, 14(2), 658-669 (2003-02-18)
Mammalian cDNA expression cloning was used to identify novel regulators of integrin-mediated cell-substratum adhesions. Using a focal adhesion morphology screen, we identified a cDNA with homology to a receptor for activated protein kinase C (RACK1) that induced a loss of
