NACA prevents short recently synthesized (i.e., nascent) ribosome-associated polypeptides from inappropriate interactions with cytosolic proteins. NACA binds nascent-polypeptide domains emerging from ribosomes unless it contains a signal peptide which is fully exposed. Depletion of NACA from ribosomes carrying nascent polypeptides allows the signal recognition particle (SRP) to crosslink to polypeptides regardless of whether or not they contain signal peptides or not. In the absence of NACA, proteins lacking signal peptides can be mis-translocated into the endoplasmic reticulum.[2][4]
The NACA protein is expressed in bone during development and acts as a transcriptional coactivator in conjunction with acidic activators.[3]
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↑Stilo R, Liguoro D, di Jeso B, Leonardi A, Vito P (April 2003). "The alpha-chain of the nascent polypeptide-associated complex binds to and regulates FADD function". Biochem. Biophys. Res. Commun. 303 (4): 1034–41. doi:10.1016/S0006-291X(03)00487-X. PMID12684039.
↑Yoshida K, Nogami S, Satoh S, Tanaka-Nakadate S, Hiraishi H, Terano A, Shirataki H (May 2005). "Interaction of the taxilin family with the nascent polypeptide-associated complex that is involved in the transcriptional and translational processes". Genes Cells. 10 (5): 465–76. doi:10.1111/j.1365-2443.2005.00848.x. PMID15836775.
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