Polyadenylate-binding protein cytoplasmic 4-like (PABPC4L)

Polyadenylate-binding protein cytoplasmic 4-like (PABPC4L) is a protein predicted to participate in mRNA regulation, particularly binding the poly(A) tail and 3'-UTR of mRNA and contributing to the formation and function of ribonucleoprotein complexes. PABPC4L is active in the cytosol, nucleus, and cytoplasmic stress granules, where it relocates in response to oxidative stress[1][5][3]. Genetic studies have linked rare truncating mutations in the PABPC4L gene to a familial form of atypical Parkinsonism, suggesting a critical role in neuronal stress response and prevention of toxic protein aggregation[3]. The protein contains four RNA recognition motifs (RRMs) typical of polyadenylate-binding proteins, and mislocalization due to a stop-gain variant disrupts stress granule dynamics, potentially contributing to neurodegeneration[3]. Currently, PABPC4L is not classified as a drug target and lacks documented pharmacological or therapeutic interactions[1][5][6].

Other names

Polyadenylate-binding protein 4-likePABPC4LPoly(A)-binding protein 4-likePABP-4-likePoly(A) binding protein cytoplasmic 4 like