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Updated: Jun 3, 2025

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里克特西亚帕克里菌与粗的内分泌网膜形成了广泛,稳定的接触

Yamilex Acevedo-Sánchez1, Patrick J Woida1, Caroline Anderson1,2

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.

The Journal of cell biology
|January 8, 2025
PubMed
概括

细菌病原体Rickettsia parkeri与宿主细胞的细胞内膜网 (ER) 形成广泛的物理接触. 这些相互作用是由ER特异性接介导的,这表明一种新的宿主-病原体通信.

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Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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