The C-terminal Dilysine Motif for Targeting to the Endoplasmic Reticulum Is Not Required for Cf-9 Function | Zendy

Renier A. L. van der Hoorn | Zendy; Anke Van der Ploeg | Zendy; P.J.G.M. de Wit | Zendy; M.H.A.J. Joosten | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

The C-terminal Dilysine Motif for Targeting to the Endoplasmic Reticulum Is Not Required for Cf-9 Function

Author(s) -

Renier A. L. van der Hoorn,

Anke Van der Ploeg,

P.J.G.M. de Wit,

M.H.A.J. Joosten

Publication year - 2001

Publication title -

molecular plant-microbe interactions

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.565

H-Index - 153

eISSN - 1943-7706

pISSN - 0894-0282

DOI - 10.1094/mpmi.2001.14.3.412

Subject(s) - endoplasmic reticulum , microbiology and biotechnology , subcellular localization , mutant , extracellular , protein sorting signals , stim1 , transport protein , biology , gene , chemistry , biochemistry , peptide sequence , signal peptide

The tomato resistance gene Cf-9 encodes a membrane-anchored, receptor-like protein that mediates specific recognition of the extracellular elicitor protein AVR9 of Cladosporium fulvum. The C-terminal dilysine motif (KKRY) of Cf-9 suggests that the protein resides in the endoplasmic reticulum. Previously, two conflicting reports on the subcellular location of Cf-9 were published. Here we show that the AARY mutant version of Cf-9 is still functional in mediating AVR9 recognition, suggesting that functional Cf-9 resides in the plasma membrane. The data presented here and in reports by others can be explained by masking the dilysine signal of Cf-9 with other proteins.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research