The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling | Zendy

Marco Biancucci | Zendy; G. Minasov | Zendy; Avik Banerjee | Zendy; Alfa Herrera | Zendy; Patrick J. Woida | Zendy; Matthew B. Kieffer | Zendy; Lakshman Bindu | Zendy; Maria Teresa AbreuBlanco | Zendy; W.F. Anderson | Zendy; Vadim Gaponenko | Zendy; Andrew Stephen | Zendy; Matthew Holderfield | Zendy; K.J.F. Satchell | Zendy

Open Access

The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling

Author(s) -

Marco Biancucci,

G. Minasov,

Avik Banerjee,

Alfa Herrera,

Patrick J. Woida,

Matthew B. Kieffer,

Lakshman Bindu,

Maria Teresa AbreuBlanco,

W.F. Anderson,

Vadim Gaponenko,

Andrew Stephen,

Matthew Holderfield,

K.J.F. Satchell

Publication year - 2018

Publication title -

science signaling

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.659

H-Index - 154

eISSN - 1937-9145

pISSN - 1945-0877

DOI - 10.1126/scisignal.aat8335

Subject(s) - mapk/erk pathway , effector , rap1 , microbiology and biotechnology , mechanism (biology) , anti apoptotic ras signalling cascade , signal transduction , endopeptidase , chemistry , biology , enzyme , biochemistry , philosophy , epistemology

A bacterial toxin effector domain disrupts RAS-ERK signaling by cleaving RAS through an unusual mechanism.

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