syntaxin

シンタキシン

関

Qa-SNARE protein

WordNet

1. the grammatical arrangement of words in sentences (同)sentence structure, phrase structure
2. a systematic orderly arrangement
3. studies of the rules for forming admissible sentences

PrepTutorEJDIC

1. 文章論,統語論,文章構成法,シンタックス(文中における語の配列を扱う文法の一部門)

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2019/06/14 21:37:05」(JST)

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Syntaxin
Structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.
Identifiers
Symbol	Syntaxin
Pfam	PF00804
InterPro	IPR006011
SMART	SM00503
SCOPe	1br0 / SUPFAM
OPM superfamily	197
OPM protein	2xhe
Membranome	349
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Syntaxins are a family of membrane integrated Q-SNARE proteins participating in exocytosis.

Domains

Syntaxins possess a single C-terminal transmembrane domain, a SNARE domain (known as H3), and an N-terminal regulatory domain (Habc). Syntaxin 17 may have two transmembrane domains.

• The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Formation of this stable SNARE core complex is believed to generate the free energy required to initiate fusion between the vesicle membrane and plasma membrane.
• The N-terminal Habc domain is formed by 3 α-helices and when collapsed onto its own H3 helix forms an inactive "closed" syntaxin conformation. This closed conformation of syntaxin is believed to be stabilized by binding of Munc-18 (nSec1), although more recent data suggests that nSec1 may bind to other conformations of syntaxin, as well. The "open" syntaxin conformation is the conformation that is competent to form into SNARE core complexes.

Function

Molecular machinery driving exocytosis in neuromediator release. The core SNARE complex is formed by four α-helices contributed by synaptobrevin, syntaxin and SNAP-25, synaptotagmin serves as a Ca²⁺ sensor and regulates intimately the SNARE zipping.

In vitro syntaxin per se is sufficient to drive spontaneous calcium independent fusion of synaptic vesicles containing v-SNAREs.

More recent and somewhat controversial amperometric data suggest that the transmembrane domain of Syntaxin1A may form part of the fusion pore of exocytosis.

Binding

Syntaxins bind synaptotagmin in a calcium-dependent fashion and interact with voltage dependent calcium and potassium channels via the C-terminal H3 domain. Direct syntaxin-channel interaction is a suitable molecular mechanism for proximity between the fusion machinery and the gates of Ca²⁺ entry during depolarization of the presynaptic axonal boutons.

The Sec1/Munc18 protein family is known to bind to Syntaxin and regulate Syntaxins machinery. Munc18-1 binds to Syntaxin 1A via two distinct sites referred as N-terminus binding and "closed" conformation that incorporates both the central Habc domain and the SNARE core domain. Munc18-1 binding to the N-terminus of Syntaxin-1 is thought to facilitate Syntaxin-1 interaction with another SNARE, while binding to the "closed" conformation of Syntaxin-1 is believed to be inhibitory.

Recently published data show that alternative spliced Syntaxin 1 (STX1B) which lacks the transmembrane domain localizes in the nuclei.

Genes

Human genes encoding syntaxin proteins include:

• STX1A, STX1B, STX2, STX3, STX4, STX5, STX6, STX7, STX8,
• STX10, STX11, STX12, STX16, STX17, STX18, STX19

See also

• Tomosyn, a syntaxin binding protein

External links

• Syntaxin at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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English Journal

• The powdery mildew resistance protein RPW8.2 is carried on VAMP721/722 vesicles to the extrahaustorial membrane of haustorial complexes.

• Kim H1, O'Connell R, Maekawa-Yoshikawa M, Uemura T, Neumann U, Schulze-Lefert P.
• The Plant journal : for cell and molecular biology.Plant J.2014 Sep;79(5):835-47. doi: 10.1111/tpj.12591. Epub 2014 Jul 23.
• Plants employ multiple cell-autonomous defense mechanisms to impede pathogenesis of microbial intruders. Previously we identified an exocytosis defense mechanism in Arabidopsis against pathogenic powdery mildew fungi. This pre-invasive defense mechanism depends on the formation of ternary protein co
• PMID 24941879

• Valosin-containing Protein-interacting Membrane Protein (VIMP) Links the Endoplasmic Reticulum with Microtubules in Concert with Cytoskeleton-linking Membrane Protein (CLIMP)-63.

• Noda C1, Kimura H1, Arasaki K1, Matsushita M1, Yamamoto A2, Wakana Y1, Inoue H1, Tagaya M3.
• The Journal of biological chemistry.J Biol Chem.2014 Aug 29;289(35):24304-13. doi: 10.1074/jbc.M114.571372. Epub 2014 Jul 9.
• The distribution and morphology of the endoplasmic reticulum (ER) in mammalian cells depend on both dynamic and static interactions of ER membrane proteins with microtubules (MTs). Cytoskeleton-linking membrane protein (CLIMP)-63 is exclusively localized in sheet-like ER membranes, typical structure
• PMID 25008318

• Cell-autonomous defense, re-organization and trafficking of membranes in plant-microbe interactions.

• Dörmann P1, Kim H, Ott T, Schulze-Lefert P, Trujillo M, Wewer V, Hückelhoven R.
• The New phytologist.New Phytol.2014 Aug 28. doi: 10.1111/nph.12978. [Epub ahead of print]
• Plant cells dynamically change their architecture and molecular composition following encounters with beneficial or parasitic microbes, a process referred to as host cell reprogramming. Cell-autonomous defense reactions are typically polarized to the plant cell periphery underneath microbial contact
• PMID 25168837

Japanese Journal

• The STX6-VTI1B-VAMP3 complex facilitates xenophagy by regulating the fusion between recycling endosomes and autophagosomes

• Autophagy 13(1), 57-69, 2017-01-02
• NAID 120006337978

• レジオネラの宿主細胞内における多彩な生存戦略の解明

• 上原記念生命科学財団研究報告集 31, 7p, 2017
• NAID 40021429106

• <b>Syntaxin 6 is Involved in the Maintenance of Secretory Granules in Parotid Acinar Cells </b>

• IJOMS 15(3-4), 67-73, 2017
• NAID 130006894939

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