{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T09:24:05Z","timestamp":1791365045662,"version":"4.3.1"},"update-to":[{"DOI":"10.1371\/journal.pgen.1010144","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2022,4,21]],"date-time":"2022-04-21T00:00:00Z","timestamp":1650499200000}}],"reference-count":65,"publisher":"Public Library of Science (PLoS)","issue":"4","license":[{"start":{"date-parts":[[2022,4,11]],"date-time":"2022-04-11T00:00:00Z","timestamp":1649635200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["CA 21765"],"award-info":[{"award-number":["CA 21765"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["NS051537"],"award-info":[{"award-number":["NS051537"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012524","name":"American Lebanese Syrian Associated Charities","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012524","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosgenetics.org"],"crossmark-restriction":false},"short-container-title":["PLoS Genet"],"abstract":"<jats:p>\n                    Polyglutamylation is a dynamic posttranslational modification where glutamate residues are added to substrate proteins by 8 tubulin tyrosine ligase-like (TTLL) family members (writers) and removed by the 6 member Nna1\/CCP family of carboxypeptidases (erasers). Genetic disruption of polyglutamylation leading to hyperglutamylation causes neurodegenerative phenotypes in humans and animal models; the best characterized being the\n                    <jats:italic>Purkinje cell degeneration<\/jats:italic>\n                    (\n                    <jats:italic>pcd<\/jats:italic>\n                    ) mouse, a mutant of the gene encoding Nna1\/CCP1, the prototypic eraser. Emphasizing the functional importance of the balance between glutamate addition and elimination, loss of TTLL1 prevents Purkinje cell degeneration in\n                    <jats:italic>pcd<\/jats:italic>\n                    . However, whether\n                    <jats:italic>Ttll1<\/jats:italic>\n                    loss protects other vulnerable neurons in\n                    <jats:italic>pcd<\/jats:italic>\n                    , or if elimination of other TTLLs provides protection is largely unknown. Here using a mouse genetic rescue strategy, we characterized the contribution of\n                    <jats:italic>Ttll1<\/jats:italic>\n                    ,\n                    <jats:italic>4<\/jats:italic>\n                    ,\n                    <jats:italic>5<\/jats:italic>\n                    ,\n                    <jats:italic>7<\/jats:italic>\n                    , or\n                    <jats:italic>11<\/jats:italic>\n                    to the degenerative phenotypes in cerebellum, olfactory bulb and retinae of\n                    <jats:italic>pcd<\/jats:italic>\n                    mutants.\n                    <jats:italic>Ttll1<\/jats:italic>\n                    deficiency attenuates Purkinje cell loss and function and reduces olfactory bulb mitral cell death and retinal photoreceptor degeneration. Moreover, degeneration of photoreceptors in\n                    <jats:italic>pcd<\/jats:italic>\n                    is preceded by impaired rhodopsin trafficking to the rod outer segment and likely represents the causal defect leading to degeneration as this too is rescued by elimination of TTLL1. Although TTLLs have similar catalytic properties on model substrates and several are highly expressed in Purkinje cells (e.g. TTLL5 and 7), besides TTLL1 only TTLL4 deficiency attenuated degeneration of Purkinje and mitral cells in\n                    <jats:italic>pcd<\/jats:italic>\n                    . Additionally, TTLL4 loss partially rescued photoreceptor degeneration and impaired rhodopsin trafficking. Despite their common properties, the polyglutamylation profile changes promoted by TTLL1 and TTLL4 deficiencies in\n                    <jats:italic>pcd<\/jats:italic>\n                    mice are very different. We also report that loss of anabolic TTLL5 synergizes with loss of catabolic Nna1\/CCP1 to promote photoreceptor degeneration. Finally, male infertility in\n                    <jats:italic>pcd<\/jats:italic>\n                    is not rescued by loss of any\n                    <jats:italic>Ttll<\/jats:italic>\n                    . These data provide insight into the complexity of polyglutamate homeostasis and function\n                    <jats:italic>in vivo<\/jats:italic>\n                    and potential routes to ameliorate disorders caused by disrupted polyglutamylation.\n                  <\/jats:p>","DOI":"10.1371\/journal.pgen.1010144","type":"journal-article","created":{"date-parts":[[2022,4,11]],"date-time":"2022-04-11T13:38:02Z","timestamp":1649684282000},"page":"e1010144","update-policy":"https:\/\/doi.org\/10.1371\/journal.pgen.corrections_policy","source":"Crossref","is-referenced-by-count":24,"title":["TTLL1 and TTLL4 polyglutamylases are required for the neurodegenerative phenotypes in pcd mice"],"prefix":"10.1371","volume":"18","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5586-8857","authenticated-orcid":true,"given":"Hui-Yuan","family":"Wu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9592-9810","authenticated-orcid":true,"given":"Yongqi","family":"Rong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Parmil K.","family":"Bansal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peng","family":"Wei","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong","family":"Guo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9659-3183","authenticated-orcid":true,"given":"James I.","family":"Morgan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2022,4,11]]},"reference":[{"key":"pgen.1010144.ref001","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/j.molcel.2007.04.012","article-title":"A Targeted Multienzyme Mechanism for Selective Microtubule Polyglutamylation","volume":"26","author":"J van Dijk","year":"2007","journal-title":"Molecular Cell"},{"key":"pgen.1010144.ref002","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/j.cell.2010.10.014","article-title":"A family of protein-deglutamylating enzymes associated with neurodegeneration","volume":"143","author":"K Rogowski","year":"2010","journal-title":"Cell."},{"key":"pgen.1010144.ref003","doi-asserted-by":"crossref","first-page":"3017","DOI":"10.1091\/mbc.e14-06-1072","article-title":"The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino 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