التفاصيل البيبلوغرافية
| العنوان: |
Structure and Function of Salmonella SifA Indicate that Its Interactions with SKIP, SseJ, and RhoA Family GTPases Induce Endosomal Tubulation. |
| المؤلفون: |
Ohlson, Maikke B., Huang, Zhiwei, Alto, Neal M., Blanc, Marie-Pierre, Dixon, Jack E., Chai, Jijie, Miller, Samuel I. |
| المصدر: |
Cell Host & Microbe; Nov2008, Vol. 4 Issue 5, p434-446, 13p |
| مصطلحات موضوعية: |
BACTERIAL proteins, SALMONELLA, GUANOSINE triphosphatase, ENDOSOMES, KINESIN, CARRIER proteins |
| مستخلص: |
Summary: The Salmonella typhimurium type III secretion effector protein SifA is essential for inducing tubulation of the Salmonella phagosome and binds the mammalian kinesin-binding protein SKIP. Coexpression of SifA with the effector SseJ induced tubulation of mammalian cell endosomes, similar to that induced by Salmonella infection. Interestingly, GTP-bound RhoA, RhoB, and RhoC also induced endosomal tubulation when coexpressed with SseJ, indicating that SifA likely mimics or activates a RhoA family GTPase. The structure of SifA in complex with the PH domain of SKIP revealed that SifA has two distinct domains; the amino terminus binds SKIP, and the carboxyl terminus has a fold similar to SopE, a Salmonella effector with Rho GTPase guanine nucleotide exchange factor activity (GEF). Similar to GEFs, SifA interacted with GDP-bound RhoA, and purified SseJ and RhoA formed a protein complex, suggesting that SifA, SKIP, SseJ, and RhoA family GTPases cooperatively promote host membrane tubulation. [Copyright &y& Elsevier] |
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