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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2025,5,27]]},"abstract":"<jats:p>\n                    Stathmin-2 (also known as\n                    <jats:italic toggle=\"yes\">SCG10<\/jats:italic>\n                    ) is encoded by the\n                    <jats:italic toggle=\"yes\">STMN2<\/jats:italic>\n                    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 proposed to function through direct binding to \u03b1\/\u03b2 tubulin heterodimers and correspondingly to affect microtubule assembly and dynamics, stathmin-2\u2019s role in axon regeneration after axotomy is shown to be independent of its tubulin binding abilities.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2502294122","type":"journal-article","created":{"date-parts":[[2025,5,20]],"date-time":"2025-05-20T13:40:02Z","timestamp":1747748402000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":23,"title":["Stathmin-2 enhances motor axon regeneration after injury independent of its binding to tubulin"],"prefix":"10.1073","volume":"122","author":[{"given":"Melinda S.","family":"Beccari","sequence":"first","affiliation":[{"name":"Department of Cellular and Molecular Medicine, University of California, San Diego","place":["La 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