메뉴 건너뛰기




Volumn 74, Issue 3, 2006, Pages 1712-1717

Endoproteolytic processing of RhoA by Rce1 is required for the cleavage of RhoA by Yersinia enterocolitica outer protein T

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL TOXIN; CYSTEINE; CYSTEINE PROTEINASE; GERANYLGERANYLCYSTEINE; GERANYLGERANYLTRANSFERASE TYPE I; ISOPRENYLCYSTEINE; ISOPRENYLCYSTEINE CARBOXYL METHYLTRANSFERASE; LIPID; MEMBRANE PROTEIN; METHYLTRANSFERASE; PROTEINASE; RAS CONVERTING ENZYME 1; RECOMBINANT PROTEIN; RHO FACTOR; RHO GUANOSINE TRIPHOSPHATASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; TRANSFERASE; UNCLASSIFIED DRUG; YERSINIA OUTER PROTEIN T;

EID: 33644784689     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.74.3.1712-1717.2006     Document Type: Article
Times cited : (16)

References (20)
  • 1
    • 0037443394 scopus 로고    scopus 로고
    • Hematologic effects of inactivating the Ras processing enzyme Rce1
    • Aiyagari, A. L., B. R. Taylor, V. Aurora, S. G. Young, and K. M. Shannon. 2003. Hematologic effects of inactivating the Ras processing enzyme Rce1. Blood 101:2250-2252.
    • (2003) Blood , vol.101 , pp. 2250-2252
    • Aiyagari, A.L.1    Taylor, B.R.2    Aurora, V.3    Young, S.G.4    Shannon, K.M.5
  • 2
    • 0032589269 scopus 로고    scopus 로고
    • Effectors for the Rho GTPases
    • Aspenstrom, P. 1999. Effectors for the Rho GTPases. Curr. Opin. Cell Biol. 11:95-102.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 95-102
    • Aspenstrom, P.1
  • 7
    • 0036792393 scopus 로고    scopus 로고
    • The Yersinia Ysc-Yop 'type III' weaponry
    • Cornelis, G. R. 2002. The Yersinia Ysc-Yop 'type III' weaponry. Nat. Rev. Mol. Cell. Biol. 3:742-752.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 742-752
    • Cornelis, G.R.1
  • 8
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S., and A. Hall. 2002. Rho GTPases in cell biology. Nature 420:629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 9
    • 0033605596 scopus 로고    scopus 로고
    • Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells
    • Kim, E., P. Ambroziak, J. C. Otto, B. Taylor, B. Ashby, K. Shannon, P. J. Casey, and S. G. Young. 1999. Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells. J. Biol. Chem. 274:8383-5390.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8383-15390
    • Kim, E.1    Ambroziak, P.2    Otto, J.C.3    Taylor, B.4    Ashby, B.5    Shannon, K.6    Casey, P.J.7    Young, S.G.8
  • 10
    • 0027518956 scopus 로고
    • Inhibitors of the isoprenylated protein endoprotease
    • Ma, Y. T., B. A. Gilbert, and R. R. Rando. 1993. Inhibitors of the isoprenylated protein endoprotease. Biochemistry 32:2386-2393.
    • (1993) Biochemistry , vol.32 , pp. 2386-2393
    • Ma, Y.T.1    Gilbert, B.A.2    Rando, R.R.3
  • 12
    • 0029805684 scopus 로고    scopus 로고
    • Tissue-specific distribution and subcellular distribution of phospholipase D in rat: Evidence for distinct RhoA- and ADP-ribosylation factor (ARF)-regulated isoenzymes
    • Provost, J. J., J. Fudge, S. Israelit, A. R. Siddiqi, and J. H. Exton. 1996. Tissue-specific distribution and subcellular distribution of phospholipase D in rat: evidence for distinct RhoA- and ADP-ribosylation factor (ARF)-regulated isoenzymes. Biochem. J. 319:285-291.
    • (1996) Biochem. J. , vol.319 , pp. 285-291
    • Provost, J.J.1    Fudge, J.2    Israelit, S.3    Siddiqi, A.R.4    Exton, J.H.5
  • 13
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • Ridley, A. J. 2001. Rho family proteins: coordinating cell responses. Trends Cell Biol. 11:471-477.
    • (2001) Trends Cell Biol. , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 14
    • 0030267458 scopus 로고    scopus 로고
    • Rho: Theme and variations
    • Ridley, A. J. 1996. Rho: theme and variations. Curr. Biol. 6:1256-1264.
    • (1996) Curr. Biol. , vol.6 , pp. 1256-1264
    • Ridley, A.J.1
  • 15
    • 0035847663 scopus 로고    scopus 로고
    • Non-peptidic, non-prenylic inhibitors of the prenyl protein-specific protease Rce1
    • Schlitzer, M., A. Winter-Vann, and P. J. Casey. 2001. Non-peptidic, non-prenylic inhibitors of the prenyl protein-specific protease Rce1. Bioorg. Med. Chem. Lett. 11:425-427.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 425-427
    • Schlitzer, M.1    Winter-Vann, A.2    Casey, P.J.3
  • 16
    • 0037417878 scopus 로고    scopus 로고
    • Biochemical characterization of the Yersinia YopT protease: Cleavage site and recognition elements in Rho GTPases
    • Shao, F., P. O. Vacratsis, Z. Bao, K. E. Bowers, C. A. Fierke, and J. E. Dixon. 2003. Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc. Natl. Acad. Sci. USA 100:904-909.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 904-909
    • Shao, F.1    Vacratsis, P.O.2    Bao, Z.3    Bowers, K.E.4    Fierke, C.A.5    Dixon, J.E.6
  • 17
    • 0035184874 scopus 로고    scopus 로고
    • Recombinant Yersinia YopT leads to uncoupling of RhoA-effector interaction
    • Sorg, I., U.-M. Goehring, K. Aktories, and G. Schmidt. 2001. Recombinant Yersinia YopT leads to uncoupling of RhoA-effector interaction. Infect. Immun. 69:7535-7543.
    • (2001) Infect. Immun. , vol.69 , pp. 7535-7543
    • Sorg, I.1    Goehring, U.-M.2    Aktories, K.3    Schmidt, G.4
  • 18
    • 0041764404 scopus 로고    scopus 로고
    • The C terminus of YopT is crucial for activity and the N terminus is crucial for substrate binding
    • Sorg, I., C. Hoffmann, J. Dumbach, K. Aktories, and G. Schmidt. 2003. The C terminus of YopT is crucial for activity and the N terminus is crucial for substrate binding. Infect. Immun. 71:4632.
    • (2003) Infect. Immun. , vol.71 , pp. 4632
    • Sorg, I.1    Hoffmann, C.2    Dumbach, J.3    Aktories, K.4    Schmidt, G.5
  • 20
    • 77956670866 scopus 로고    scopus 로고
    • Postisoprenylation protein processing: CXXX (CaaX) endoproteases and isoprenylcysteine carboxyl methyltransferase
    • F. Tamanoi and D. S. Sigman (ed.). Academic Press, San Diego, Calif.
    • Young, S. G., P. Ambroziak, E. Kim, and S. Clarke. 2000. Postisoprenylation protein processing: CXXX (CaaX) endoproteases and isoprenylcysteine carboxyl methyltransferase, p. 155-213. In F. Tamanoi and D. S. Sigman (ed.), The enzymes, vol. 21. Academic Press, San Diego, Calif.
    • (2000) The Enzymes , vol.21 , pp. 155-213
    • Young, S.G.1    Ambroziak, P.2    Kim, E.3    Clarke, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.