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Striatin-4 (STRN4) is a calmodulin-binding scaffolding protein at the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes, acting as a regulatory subunit of protein phosphatase 2A (PP2A)[1][3][4][8]. STRN4 does not have intrinsic catalytic activity but organizes large, multisubunit signaling complexes crucial for the regulation of diverse cellular processes, including signal transduction, cell growth, differentiation, cytoskeleton remodeling, apoptosis, metabolism, and immune responses[2][3][8]. It is particularly involved in the negative regulation of Hippo signaling and interacts with various kinases, including germinal center kinase III family members[1][2]. STRN4 is broadly expressed, especially in brain and reproductive organs[7][9], and has been implicated in several diseases such as muscular dystrophy-dystroglycanopathy, cerebral cavernous malformation, cardiac diseases, and potentially others[1][2]. To date, no direct drug interactions or established biomarker or safety concern roles have been described in the literature. STRN4 is best understood as a scaffolding or adaptor protein, not as a classic therapeutic target such as an enzyme, receptor, transporter, or ion channel[2][3][1]. There are currently no known drugs or inhibitors directly targeting STRN4, nor is it a prominent clinical biomarker or common drug safety concern in published sources. All primary aliases and major molecular/functional information are from authoritative databases including UniProt, GeneCards, and HGNC[1][4][8][9].
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