. . . . . . . . "Septins are a group of GTP-binding proteins expressed in all eukaryotic cells except plants. Different septins form protein complexes with each other. These complexes can further assemble into filaments, rings and gauzes. Assembled as such, septins function in cells by localizing other proteins, either by providing a scaffold to which proteins can attach, or by forming a barrier preventing the diffusion of molecules from one compartment of the cell to another, or in the cell cortex as a barrier to the diffusion of membrane-bound proteins. Septins have been implicated in the localization of cellular processes at the site of cell division, and at the cell membrane at sites where specialized structures like cilia or flagella are attached to the cell body. In yeast cells, they compartmentalize parts of the cell and build scaffolding to provide structural support during cell division at the septum, from which they derive their name. Research in human cells suggests that septins build cages around pathogenic bacteria, that immobilize and prevent them from invading other cells. As filament forming proteins, septins can be considered part of the cytoskeleton. Apart from forming non-polar filaments, septins associate with cell membranes, the cell cortex, actin filaments and microtubules."@en . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . "Septinas s\u00E3o prote\u00EDnas que atuam no est\u00E1gio final da divis\u00E3o celular. Foram descobertas em 1970 por Leland H. Hartwell em estudos de fungos na fase da citocinese. O radical \"sept\" foi adotado para lembrar a forma\u00E7\u00E3o do septo, que faz o estrangulamento no final da divis\u00E3o, separando em duas partes o conte\u00FAdo citoplasm\u00E1tico. Resultados laboratoriais revelaram quatro mutantes que impediam a ocorr\u00EAncia natural da citocinese a certas temperaturas. Os genes correspondentes representam as quatro primeiras septinas, ScCDC3, ScCDC10, ScCDC11 e ScCDC12. A sigla \"ScCDC\" refere-se ao fungo usado nas experi\u00EAncias, Sc \u2013 Saccharomyces cerevisiae. As letras CDC significam \"Cell Division Cycle\" (Ciclo da Divis\u00E3o Celular), e tornou-se um c\u00F3digo para diversas prote\u00EDnas detectadas nas investiga\u00E7\u00F5es do grupo de Leland; a signific\u00E2ncia e a quantidade de novas descobertas deste trabalho renderam a este c\u00E9lebre cientista, juntamente com Paul Nurse e Tim Hunt, o Pr\u00EAmio Nobel de Fisiologia em 2001. No caso especial de septinas humanas e de peixes, popularizou-se uma nova nomenclatura, com todas as letras mai\u00FAsculas: SEPT1, SEPT2, SEPT3, ..., SEPT14, e assim sucessivamente, conforme novas forem descobertas. As septinas se organizam em filamentos e tamb\u00E9m como um grande anel, cujo di\u00E2metro diminui gradualmente, espremendo a c\u00E9lula. A mitose estar\u00E1 conclu\u00EDda quando o di\u00E2metro do anel de septinas se tornar t\u00E3o pequeno que cada c\u00E9lula filha possuir\u00E1 sua pr\u00F3pria membrana plasm\u00E1tica. J\u00E1 n\u00E3o se fala mais em um citoplasma, mas dois, totalmente separados pela fronteira membranar rec\u00E9m-criada. Neste momento, as septinas se desorganizam, se desfazem e s\u00E3o digeridas. Os amino\u00E1cidos s\u00E3o reciclados. Diversas outras fun\u00E7\u00F5es foram associadas a septinas. Notava-se que, embora houvesse certa diversidade funcional delas, uma caracter\u00EDstica parecia estar sempre presente: em todas as observa\u00E7\u00F5es, elas formavam complexos filamentares que impediam a mistura de conte\u00FAdos. Em outras palavras, elas participavam da cria\u00E7\u00E3o de divisores de ambientes, membranas. \u00C9 o caso da citocinese, da exocitose e da esporula\u00E7\u00E3o. Mais recentemente, septinas foram identificadas no tecido cerebral humano. O assunto \u00E9 de crescente interesse na comunidade cient\u00EDfica, j\u00E1 que septinas foram inclu\u00EDdas no grupo de prote\u00EDnas que sofrem muta\u00E7\u00F5es em causa ou consequ\u00EAncia de doen\u00E7as neurodegenerativas, como Alzheimer e Parkinson, al\u00E9m de alguns tipos de c\u00E2ncer e infertilidade masculina. O genoma humano indica a presen\u00E7a de pelo menos treze genes que codificam septinas. As prote\u00EDnas produzidas por esses treze genes s\u00E3o agrupadas por homologia de sequ\u00EAncia em quatro subgrupos, cada um denominado pela septina fundadora do grupo: (i) SEPT2 (SEPT1, SEPT4, SEPT5), (ii) SEPT3 (SEPT9, SEPT12), (iii) SEPT6 (SEPT8, SEPT10, SEPT11, SEPT14), e (iv) SEPT7. Grande maioria delas t\u00EAm partes de suas estruturas cristalogr\u00E1ficas depositadas no \"PDB\" e somente duas (SEPT10 e SEPT14) n\u00E3o possuem estrutura elucidada. Uma septina humana pode ser dividida em tr\u00EAs regi\u00F5es bem definidas: o N-terminal, o dom\u00EDnio ligador de GTP e o C-terminal (que cont\u00E9m sequ\u00EAncias coiled coil). Membros do subgrupo SEPT6 s\u00E3o os \u00FAnicos que n\u00E3o apresentam atividade GTPase. Apesar da maioria dos cristais obtidos sejam do dom\u00EDnio ligador de GTP, algumas estruturas dos dom\u00EDnios C-terminais tamb\u00E9m est\u00E3o dispon\u00EDveis. A septina 2 forma homod\u00EDmeros e foi estudada inicialmente por dois grupos de cientistas, usando difra\u00E7\u00E3o de raios X. Na Universidade de Oklahoma, Estados Unidos, Wael M. Rabeh e colaboradores obtiveram resolu\u00E7\u00E3o de 2,6 \u00C5. No Instituto Max Planck em Dortmund, Alemanha, Minhajuddin Sirajuddin et al. conseguiram resolu\u00E7\u00E3o de 3,4 \u00C5. Estes \u00FAltimos tamb\u00E9m apresentaram um heterotr\u00EDmero formado pelas septinas 2, 6 e 7, com resolu\u00E7\u00E3o de 4,0 \u00C5, conforme publica\u00E7\u00E3o da revista Nature. Uma septina de subgrupos diferentes se juntam de forma organizada, criando um complexo linear sim\u00E9trico. Esse complexo em humanos pode ser (6 subunidades; uma septina de tr\u00EAs subgrupos diferentes, com duas c\u00F3pias cada) ou (8 subunidades; quando um membro do subgrupo SEPT3 \u00E9 inclu\u00EDdo) e \u00E9 a estrutura b\u00E1sica na forma\u00E7\u00E3o de filamentos. Mais recentemente foi corrigida a ordem das subunidades de septina: SEPT2-SEPT6-SEPT7-SEPT3-SEPT3-SEPT7-SEPT6-SEPT2 ou SEPT2-SEPT6-SEPT7-SEPT7-SEPT6-SEPT2 no caso de complexos (antes acreditava-se que a ordem seria SEPT7-SEPT6-SEPT2-SEPT2-SEPT6-SEPT7). Filamentos longos s\u00E3o ent\u00E3o formados, atrav\u00E9s da polimeriza\u00E7\u00E3o ponta-a-ponta desses complexos hetero-oligom\u00E9ricos. No Brasil, h\u00E1 um grupo de pesquisa sobre septinas, sediado no Instituto de F\u00EDsica de S\u00E3o Carlos (USP). Os primeiros estudos foram conduzidos pelo Centro de Biotecnologia Molecular e Estrutural (CBME), um dos primeiros projetos de inova\u00E7\u00E3o e difus\u00E3o criados pela FAPESP cujas atividades iniciaram em 2001. O grupo s\u00E3ocarlense, coordenado pelo , elucidou a maioria das estruturas de septinas dispon\u00EDvel at\u00E9 hoje, inclusive septinas de outros organismos como Schistosoma mansoni e Chlamydomonas reinhardtii. Recentemente, tamb\u00E9m no Instituto de F\u00EDsica de S\u00E3o Carlos, foram resolvidas as estruturas da regi\u00E3o coiled coil da septina 4 e do dom\u00EDnio GTPase da septina 7, com resolu\u00E7\u00F5es de 1,35 e 1,74 \u00C5, respectivamente. Estas s\u00E3o as melhores resolu\u00E7\u00F5es obtidas para septinas at\u00E9 hoje."@pt . . . . . . . . . . . "Septin"@en . . . . . . "CL0023"@en . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . "Septinas s\u00E3o prote\u00EDnas que atuam no est\u00E1gio final da divis\u00E3o celular. Foram descobertas em 1970 por Leland H. Hartwell em estudos de fungos na fase da citocinese. O radical \"sept\" foi adotado para lembrar a forma\u00E7\u00E3o do septo, que faz o estrangulamento no final da divis\u00E3o, separando em duas partes o conte\u00FAdo citoplasm\u00E1tico. Resultados laboratoriais revelaram quatro mutantes que impediam a ocorr\u00EAncia natural da citocinese a certas temperaturas. Os genes correspondentes representam as quatro primeiras septinas, ScCDC3, ScCDC10, ScCDC11 e ScCDC12."@pt . . . . . . . . . . . . . . "Septina"@pt . . . "Septinak lotura duten proteinak dira eta Zelula eukariotoetako (landare zelulak ezik) zitoeskeletoaren laugarren osagai kontsideratzen dira. Septina desberdinek proteina konplexuak osaratzen dituzte eta gainerako zuntzekin elkartuz eraztun antzeko egiturak eratzen dituzte."@eu . . . . . . . . . . "Septina"@eu . . . . . . . . . . . . . . . . . . . "Cell_Div_GTP_bd" . "Las septinas (del ingl\u00E9s \"septins\"), consideradas el cuarto componente del citoesqueleto,\u200B fueron descritas en levaduras gemantes de Saccharomyces cerevisiae como filamentos en el cuello de la levadura madre, estas observaciones fueron realizadas durante estudios de control gen\u00E9tico del ciclo de divisi\u00F3n celular.\u200B Prote\u00EDnas con secuencias hom\u00F3logas han sido identificadas en c\u00E9lulas eucariotas desde levaduras hasta animales incluyendo al hombre, pero no han sido descritas en plantas.\u200B En bacterias, las paraseptinas son prote\u00EDnas relacionadas con las septinas, estas \u00FAltimas se especula que fueron adquiridas por las c\u00E9lulas eucariotas por transferencia lateral de bacterias.\u200B El n\u00FAmero de genes que codifican para septinas var\u00EDa ampliamente entre los diferentes organismos, por ejemplo para Caen"@es . . . . . . . . "Cell division/GTP binding protein"@en . . "28001"^^ . . . . . . . . . . . . . "Las septinas (del ingl\u00E9s \"septins\"), consideradas el cuarto componente del citoesqueleto,\u200B fueron descritas en levaduras gemantes de Saccharomyces cerevisiae como filamentos en el cuello de la levadura madre, estas observaciones fueron realizadas durante estudios de control gen\u00E9tico del ciclo de divisi\u00F3n celular.\u200B Prote\u00EDnas con secuencias hom\u00F3logas han sido identificadas en c\u00E9lulas eucariotas desde levaduras hasta animales incluyendo al hombre, pero no han sido descritas en plantas.\u200B En bacterias, las paraseptinas son prote\u00EDnas relacionadas con las septinas, estas \u00FAltimas se especula que fueron adquiridas por las c\u00E9lulas eucariotas por transferencia lateral de bacterias.\u200B El n\u00FAmero de genes que codifican para septinas var\u00EDa ampliamente entre los diferentes organismos, por ejemplo para Caenorhabditis elegans se conocen 2, en Encephalitozoon cuniculi 3, en Drosophila melanogaster 5, S. cerevisiae 7, Homo sapiens 14 y en Danio rerio (Pez cebra) 17.\u200B Las septinas son un grupo de prote\u00EDnas que contienen una regi\u00F3n conservada de uni\u00F3n a GTP, adem\u00E1s todas estas prote\u00EDnas pueden formar complejos heterom\u00E9ricos, los cuales se asocian con un alto grado de orden estructural. Por ejemplo, filamentos, anillos y horquillas en forma de reloj de arena\u200B los cuales se localizan en el sitio de divisi\u00F3n de la membrana plasm\u00E1tica, en los anillos de los espermatozoides y en la base de los cilios y dendritas. Las septinas tambi\u00E9n pueden asociarse con los filamentos de actina, microt\u00FAbulos y con fosfol\u00EDpidos de la membrana.\u200B Sin embargo, al igual que los filamentos intermedios, las septinas no presentan polaridad. Aunque se cree que no contribuyen en la generaci\u00F3n de fuerza contr\u00E1ctil, se tiene evidencia de su participaci\u00F3n en diferentes procesos celulares como la citog\u00E9nesis, ciliog\u00E9nesis, neurog\u00E9nesis, migraci\u00F3n celular, mitosis, crecimiento y polarizaci\u00F3n de las c\u00E9lulas. Las septinas act\u00FAan como andamio y participan en el reclutamiento y organizaci\u00F3n de prote\u00EDnas, actuando como barrera de difusi\u00F3n para separar distintos dominios en las membranas\u200B1, evitando la difusi\u00F3n de factores de la citocinesis, prote\u00EDnas y RNAs ente la c\u00E9lula madre e hija.\u200B El mal funcionamiento de estas prote\u00EDnas est\u00E1 relacionado con enfermedades neurodegenerativas (Alzheimer y Parkinson), c\u00E1ncer (colon, oral, leucemias) e infertilidad masculina;\u200B por lo cual es importante el estudio de estas prote\u00EDnas como componentes del citoesqueleto."@es . "\u30BB\u30D7\u30C1\u30F3"@ja . . . . "Septina"@es . . . . . . . . . . . . . . . . . . . . "8299558"^^ . . . . "Septins are a group of GTP-binding proteins expressed in all eukaryotic cells except plants. Different septins form protein complexes with each other. These complexes can further assemble into filaments, rings and gauzes. Assembled as such, septins function in cells by localizing other proteins, either by providing a scaffold to which proteins can attach, or by forming a barrier preventing the diffusion of molecules from one compartment of the cell to another, or in the cell cortex as a barrier to the diffusion of membrane-bound proteins."@en . . . . . . . "Septinak lotura duten proteinak dira eta Zelula eukariotoetako (landare zelulak ezik) zitoeskeletoaren laugarren osagai kontsideratzen dira. Septina desberdinek proteina konplexuak osaratzen dituzte eta gainerako zuntzekin elkartuz eraztun antzeko egiturak eratzen dituzte."@eu . . "IPR000038"@en . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . "1045088148"^^ . . 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"PF00735"@en . . . "Cell_Div_GTP_bd"@en . . . 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