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Vol. 11, Issue 8, 2529-2542, August 2000
*Département de Pathologie et Biologie Cellulaire,
Faculté de Médecine, Université de Montréal,
Montréal, Québec, Canada, H3C 3J7; 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
ccDepartment
of Anatomy and Cell Biology, McGill University, Montreal, Quebec,
Canada, H3A 2B2; Zentrum fur Molekulare Biologie der
Universitat Heidelberg, 69052 Heidelberg, Germany;
§Department of Medicinal Chemistry and Molecular
Pharmacology, Purdue University, West Lafayette, Indiana, 47907-1333;
Clinical Sciences Unit, The Queensland Institute of
Medical Research, PO Royal Brisbane Hospital, Brisbane, Queensland
4029, Australia; and ¶Institute of Molecular and Cell
Biology, Singapore 117609, Singapore
1) isolated from rat liver homogenates
reconstitute tER by Mg2+GTP- and
Mg2+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.
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