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SMN interacts with a novel family of hnRNP and spliceosomal proteins
Author(s) -
Mourelatos Zissimos,
Abel Linda,
Yong Jeongsik,
Kataoka Naoyuki,
Dreyfuss Gideon
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.19.5443
Subject(s) - biology , snrnp , rna splicing , spinal muscular atrophy , ribonucleoprotein , heterogeneous nuclear ribonucleoprotein , exonic splicing enhancer , alternative splicing , microbiology and biotechnology , small nuclear ribonucleoprotein , genetics , heterogeneous ribonucleoprotein particle , rna binding protein , exon , messenger rna , gene , rna
Spinal muscular atrophy (SMA) is a common neurodegenerative disease caused by deletion or loss‐of‐function mutations of the survival of motor neurons (SMN) protein. SMN is in a complex with several proteins, including Gemin2, Gemin3 and Gemin4, and it plays important roles in small nuclear ribonucleoprotein (snRNP) biogenesis and in pre‐mRNA splicing. Here, we characterize three new hnRNP proteins, collectively referred to as hnRNP Qs, which are derived from alternative splicing of a single gene. The hnRNP Q proteins interact with SMN, and the most common SMN mutant found in SMA patients is defective in its interactions with them. We further demonstrate that hnRNP Qs are required for efficient pre‐mRNA splicing in vitro . The hnRNP Q proteins may provide a molecular link between the SMN complex and splicing.