High impact information on Stx5a

• Here, syntaxin 5 (Syn5) was shown to be an integral component of endoplasmic reticulum-derived transport vesicles [1].
• The ATPase associated with different cellular activities family member p97, associated p47, and the t-SNARE syntaxin 5 are necessary for the cell-free reconstitution of transitional endoplasmic reticulum (tER) from starting low-density microsomes [2].
• We conclude that the PCTV-cis-Golgi SNARE complex is composed of VAMP7, syntaxin 5, Bet1, and vti1a [3].
• Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic reticulum [4].
• The early Golgi t-SNARE (target-membrane-associated soluble-N-ethylmaleimide-sensitive factor attachment protein receptor) syntaxin 5 is thought to specify the docking site for both COPI and COPII coated vesicles originating from the endoplasmic reticulum (ER) and COPI vesicles on the retrograde pathway [5].

Biological context of Stx5a

• In the NAc shell, morphine administration resulted in upregulation of caspace 9, NF-kappaB, NF-H, tau, GABA-A delta subunit, FGFR1, Ggamma2, synuclein 1, syntaxin 5 and 13, GRK5, and c-fos mRNAs [6].

Anatomical context of Stx5a

• To extend these observations we have now cloned a protein from rat liver membranes which forms a native complex with syntaxin 5 [7].
• Additionally, we find that syntaxins 6, 7 and 8, but not syntaxin 5, are present at the plasma membrane, and that these syntaxins cycle through the plasma membrane by virtue of their cytoplasmic domains [8].

Associations of Stx5a with chemical compounds

• Previously it had been shown that p97-mediated reassembly of Golgi cisternae from mitotic Golgi fragments requires p47 which mediates the binding of p97 to a Golgi t-SNARE (soluble N-ethylmaleimide-sensitive factor attachment factor receptor), syntaxin 5 [9].

Physical interactions of Stx5a

• Three-dimensional structure of the rSly1 N-terminal domain reveals a conformational change induced by binding to syntaxin 5 [10].

Other interactions of Stx5a

• Comparison with the crystal structure of a complex between Sly1p and Sed5p, their yeast homologues, shows that syntaxin 5 binding requires a striking conformational change involving a two-residue shift in the register of the C-terminal beta-strand of rSly1N [10].
• Here we demonstrate that hsc70 chaperones stimulate in vitro SNARE complex formation among the ER/Golgi SNAREs syntaxin 5, membrin, rbetl and sec22b, under conditions in which assembly is normally inhibited [11].

References