p97和Syntaxin 5在内质网过渡态组装中的作用。
Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic reticulum.
作者信息
Roy L, Bergeron J J, Lavoie C, Hendriks R, Gushue J, Fazel A, Pelletier A, Morré D J, Subramaniam V N, Hong W, Paiement J
机构信息
Département de Pathologie et Biologie Cellulaire, Faculté de Médecine, Université de Montréal, Québec, Canada.
出版信息
Mol Biol Cell. 2000 Aug;11(8):2529-42. doi: 10.1091/mbc.11.8.2529.
Transitional endoplasmic reticulum (tER) consists of confluent rough and smooth endoplasmic reticulum (ER) domains. In a cell-free incubation system, low-density microsomes (1.17 g cc(-1)) isolated from rat liver homogenates reconstitute tER by Mg(2+)GTP- and Mg(2+)ATP-hydrolysis-dependent membrane fusion. The ATPases associated with different cellular activities protein p97 has been identified as the relevant ATPase. The ATP depletion by hexokinase or treatment with either N-ethylmaleimide or anti-p97 prevented assembly of the smooth ER domain of tER. High-salt washing of low-density microsomes inhibited assembly of the smooth ER domain of tER, whereas the readdition of purified p97 with associated p47 promoted reconstitution. The t-SNARE syntaxin 5 was observed within the smooth ER domain of tER, and antisyntaxin 5 abrogated formation of this same membrane compartment. Thus, p97 and syntaxin 5 regulate assembly of the smooth ER domain of tER and hence one of the earliest membrane differentiated components of the secretory pathway.
过渡性内质网（tER）由融合的粗面和滑面内质网（ER）结构域组成。在无细胞孵育系统中，从大鼠肝脏匀浆中分离出的低密度微粒体（1.17 g cc(-1)）通过Mg(2+)GTP和Mg(2+)ATP水解依赖性膜融合来重构tER。与不同细胞活动相关的ATP酶蛋白p97已被鉴定为相关的ATP酶。己糖激酶消耗ATP或用N-乙基马来酰亚胺或抗p97处理可阻止tER滑面内质网结构域的组装。对低密度微粒体进行高盐洗涤会抑制tER滑面内质网结构域的组装，而重新添加纯化的p97和相关的p47则可促进重构。在tER的滑面内质网结构域中观察到t-SNARE syntaxin 5，抗syntaxin 5可消除同一膜区室的形成。因此，p97和syntaxin 5调节tER滑面内质网结构域的组装，从而调节分泌途径中最早的膜分化成分之一。
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