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Comment
. 2005 Feb 1;102(5):1271-2.
doi: 10.1073/pnas.0409531101. Epub 2005 Jan 26.

Bacterial subversion of the host secretory pathway

Craig R Roy  1
Affiliations
Comment

Bacterial subversion of the host secretory pathway

Craig R Roy. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 1.
Fig. 1.
Vacuoles containing Brucella and Legionella converge on the secretory pathway at different stages. (A) Sar-1 activation leads to the recruitment of the CopII coat complex to ER membranes. CopII recruits cargo that is to be delivered to other organelles and packages the cargo into membrane tubules and vesicles. In cells producing Sar-1[T39N], CopII recruitment to membranes is inhibited, and ER exit sites do not function. In cells producing Sar-1[H79G] protein or Arf[T31N] protein, ER exit sites are functional, but cargo is not transported away from the ER. (B) Arf activation leads to the recruitment of the CopI coat complex to early secretory vesicles. The exchange of the CopII coat for the CopI coat on these membranes allows further protein sorting to occur on these vesicles and transport of cargo away from the ER. Cells are able to assemble a functional Golgi apparatus, and the secretory pathway is fully operational. (C) Vacuoles containing Brucella require the activities of the Sar-1/CopII system for productive interactions with the ER. Cells producing the Sar-1[T39N] protein are nonpermissive for Brucella replication. (D) Vacuoles containing Legionella require the sequential activities of the Sar-1/CopII system and the Arf/CopI system for productive interactions with the ER. Cells producing either Sar-1[H79G] or Arf[T31N] are nonpermissive for Legionella replication.
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