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Signal recognition particle 68 kDa subunit (SRP68) is a protein coding gene that encodes a core subunit of the signal recognition particle (SRP), a ribonucleoprotein complex universally conserved in eukaryotes[1]. The SRP recognizes and targets secretory and membrane proteins to the endoplasmic reticulum (ER) for co-translational translocation[1][2]. SRP68 forms a heterodimer with SRP72 and, together with other subunits and the 7SL RNA scaffold, is essential for the SRP’s function in arresting translation elongation, guiding the ribosome-nascent chain complex to the ER membrane, and facilitating nascent protein translocation into the ER lumen[1][2][3]. Mutations or deficiencies in SRP68 (and other SRP subunits) disrupt protein targeting, leading to activation of quality control mechanisms (e.g., RAPP), mRNA degradation of affected proteins, and a range of diseases including congenital neutropenia, cancer, and autoimmune disorders[3]. In cancer, SRP68, along with other SRP components, can contribute to tumor progression by attenuating the tumor suppressor p53, thus promoting cell survival and proliferation[3]. SRP68 is not currently a direct therapeutic target, but its pathway is essential for normal cell physiology and is implicated in multiple disease states when disrupted[3].
null (as of current knowledge, SRP68 is not a direct drug target and there are no drugs with a known mechanism of action against SRP68 specifically; SRP pathway disruption broadly affects protein targeting and quality control pathways)
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