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Edinburgh, Scotland, United Kingdom - TAIR

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Endocytic trafficking: New players in FLS2/<br />

flagellin signaling<br />

Cell surface receptor kinases serve as sensors for internal and external stimuli<br />

that trigger signaling cascades and are evidently important for developmental<br />

regulation and self from non-self discrimination. Active defenses are initiated<br />

upon receptor-mediated perception of so-called pathogen-associated molecular<br />

patterns (PAMPs). One of the best-studied PAMPs is bacterial flagellin (flg22),<br />

which is recognized by the receptor kinase Flagellin Sensing 2 (FLS2). Upon<br />

flg22 sensing, FLS2 elicits an array of defense responses, which enhance plant<br />

immunity to prevent bacterial infection and proliferation. Concomitantly, activated<br />

FLS2 translocates to an endosomal pool reminiscent of receptor-mediated<br />

endocytosis. Although both, PAMP perception and receptor trafficking became<br />

a focus of research in the past years, there is largely nothing known about<br />

downstream molecules of receptor signaling and regulatory components of<br />

receptor endocytosis.<br />

To identify such components we searched for FLS2 Interacting Proteins (FIPs)<br />

by yeast split-ubiquitin screening. FIP1 is a member of a gene family encoding<br />

transmembrane proteins, which potentially regulate cellular Ca2+ levels. Using<br />

chemical interference we showed that flg22-triggered FLS2 endocytosis requires<br />

changes in the Ca2+ distribution. FIP1-GFP was clearly localized to the plasma<br />

membrane and notably, was internalized into endosomes upon flg22 treatment.<br />

We will further discuss in planta interaction and co-localization of FLS2 and FIP1.<br />

Moreover, mutant plants devoid of FIP1 and its close homologue FIP1-like are<br />

impaired in flg22-triggered responses, which was confirmed by chemical<br />

inhibition of FIP1 activity. This suggests that FIP1 is a critical component of<br />

FLS2 signaling. A detailed characterization of fip1/fip1-like phenotypes will be<br />

presented. Unlike FIP1, FIP2 appeared to mostly localize to the cytoplasm. It<br />

codes for a soluble kinase and currently, we are addressing the relevance of<br />

FIP2 in FLS2 signaling and endocytosis.<br />

77<br />

C26<br />

Thursday 15:00 - 15:15<br />

Plant Defence<br />

Nicolas Frei dit Frey<br />

Stephanie Laurent<br />

Denise Altenbach<br />

Silke Robatzek<br />

Max-Planck-Institute for<br />

Plant Breeding Research<br />

Carl-von-Linne-Weg 10<br />

50829 Cologne<br />

Germany

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