{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Beccari MS"],"funding":["NOMIS Stiftung (NOMIS Foundation)","NIA NIH HHS","HHS | NIH | National Institute of Neurological Disorders and Stroke (NINDS)","Muscular Dystrophy Association (MDA)","HHS | NIH | National Institute on Aging (NIA)","NINDS NIH HHS","HHS | NIH | National Institute of General Medical Sciences (NIGMS)","NIGMS NIH HHS"],"pagination":["e2502294122"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12130871"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["122(21)"],"pubmed_abstract":["Stathmin-2 (also known as <i>SCG10</i>) is encoded by the <i>STMN2</i> gene, whose mRNA is one of the most abundantly expressed in human motor neurons. In almost all instances of ALS and other TDP-43 proteinopathies, stathmin-2 encoding mRNAs are cryptically spliced and polyadenylated in motor neurons, a pathogenic consequence of nuclear loss of function of the RNA binding protein TDP-43. While stathmin-2 has been shown to enhance regeneration after axonal injury to axons of cultured motor neurons, here, we show that after crush injury within the adult murine nervous system of wild-type or stathmin-2-null mice, the presence of stathmin-2 reduces axonal and neuromuscular junction degeneration and stimulates reinnervation and functional recovery. Mechanistically, although stathmin-2 has been"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Stathmin-2 enhances motor axon regeneration after injury independent of its binding to tubulin."],"pmcid":["PMC12130871"],"funding_grant_id":["N/A","RF1NS124203","R01 NS124203","RF1 NS124203","R35GM144121","T32 GM008666","R35 GM144121","T32AG066596","P30 NS047101","T32GM008666","T32 AG066596","R01 NS112503","R01NS112503","P30NS047101"],"pubmed_authors":["Kim DH","Lutz CM","Cleveland DW","Murgia-Bay B","Lagier-Tourenne C","Arnold-Garcia O","Baughn MW","Corbett KD","McAlonis-Downes M","Artates JW","Leyva-Cazares DF","Rangel CK","Beccari MS","Lim J","Lopez-Erauskin J","Melamed Z","Bernal-Buenrostro CN","Rubio-Lara HI","Ramirez-Rodriguez A"],"additional_accession":[]},"is_claimable":false,"name":"Stathmin-2 enhances motor axon regeneration after injury independent of its binding to tubulin.","description":"Stathmin-2 (also known as <i>SCG10</i>) is encoded by the <i>STMN2</i> gene, whose mRNA is one of the most abundantly expressed in human motor neurons. In almost all instances of ALS and other TDP-43 proteinopathies, stathmin-2 encoding mRNAs are cryptically spliced and polyadenylated in motor neurons, a pathogenic consequence of nuclear loss of function of the RNA binding protein TDP-43. While stathmin-2 has been shown to enhance regeneration after axonal injury to axons of cultured motor neurons, here, we show that after crush injury within the adult murine nervous system of wild-type or stathmin-2-null mice, the presence of stathmin-2 reduces axonal and neuromuscular junction degeneration and stimulates reinnervation and functional recovery. Mechanistically, although stathmin-2 has been","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-07-15T07:34:23.611Z","creation":"2026-07-02T03:08:47.842Z"},"accession":"S-EPMC12130871","cross_references":{"pubmed":["40392845"],"doi":["10.1073/pnas.2502294122"]}}