A Sintaxina 1A (STX1A ou STX1) é unha proteína codificada nos humanos no xene STX1A do cromosoma 7, que intervén na fusión de membranas durante a exocitose.[1]
As vesículas sinápticas almacenan neurotransmisores que son liberados durante a exocitose regulada polo calcio. A especificidade da liberación do neurotransmisor require a localización das vesículas sinápticas e dos canles de calcio na zona activa presináptica. As sintaxinas actúan neste proceso de fusión de vesículas.
A sintaxina 1A é un membro da superfamilia da sintaxina. As sintaxinas son proteínas específicas do sistema nervioso implicadas no atraque de vesículas sinápticas na membrana plasmática presináptica. As sintaxinas posúen un só dominio C-terminal transmembrana, un dominio SNARE (chamado H3), e un dominio regulador N-terminal (Habc). As sintaxinas únense á sinaptotagmina dun modo dependente do calcio e interaccionan con canles de calcio e potasio reguladas por voltaxe por medio do seu dominio C-terminal H3. A sintaxina 1A é unha proteína clave na regulación do canle iónica e na exocitose sináptica.[2]
As sintaxinas serven como substrato para a neurotoxina botúlica tipo C, unha metaloprotease que bloquea a exocitose e ten unha alta afinidade por un complexo molecular no que está incluído o receptor de alfa-latrotoxina, que produce unha exocitose explosiva.[3]
O nivel de expresión de STX1A está correlacionado directamente coa intelixencia na síndrome de Williams.[4]
STX1A presenta interaccións con:
- CPLX1,[5][6][7]
- CFTR,[8][9]
- NAPA,[10][11]
- RNF40,[12]
- SCNN1G,[13]
- SLC6A1,[14][15][16]
- SNAP-25,[5][6][10][17][18][19][20][21][22][23][24]
- SNAP23,[22][24][25][26][27]
- STXBP1,[5][10][18][28][29]
- STXBP5,[30][31]
- SYT1[32][33]
- UNC13B,[34]
- VAMP2,[5][6][10][29][35][36] e
- VAMP8.[37]
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