PMID- 19000165
OWN - NLM
STAT- MEDLINE
DCOM- 20090330
LR  - 20240109
IS  - 1365-313X (Electronic)
IS  - 0960-7412 (Linking)
VI  - 57
IP  - 6
DP  - 2009 Mar
TI  - Extracellular transport and integration of plant secretory proteins into 
      pathogen-induced cell wall compartments.
PG  - 986-99
LID - 10.1111/j.1365-313X.2008.03743.x [doi]
AB  - Many fungal parasites enter plant cells by penetrating the host cell wall and, 
      thereafter, differentiate specialized intracellular feeding structures, called 
      haustoria, by invagination of the plant's plasma membrane. Arabidopsis PEN gene 
      products are known to act at the cell periphery and function in the execution of 
      apoplastic immune responses to limit fungal entry. This response underneath 
      fungal contact sites is tightly linked with the deposition of plant cell wall 
      polymers, including PMR4/GSL5-dependent callose, in the paramural space, thereby 
      producing localized wall thickenings called papillae. We show that powdery mildew 
      fungi specifically induce the extracellular transport and entrapment of the 
      fusion protein GFP-PEN1 syntaxin and its interacting partner monomeric yellow 
      fluorescent protein (mYFP)-SNAP33 within the papillary matrix. Remarkably, 
      PMR4/GSL5 callose, GFP-PEN1, mYFP-SNAP33, and the ABC transporter GFP-PEN3 are 
      selectively incorporated into extracellular encasements surrounding haustoria of 
      the powdery mildew Golovinomyces orontii, suggesting that the same secretory 
      defense responses become activated during the formation of papillae and 
      haustorial encasements. This is consistent with a time-course analysis of the 
      encasement process, indicating that these extracellular structures are generated 
      through the extension of papillae. We show that PMR4/GSL5 callose accumulation in 
      papillae and haustorial encasements occurs independently of PEN1 syntaxin. We 
      propose a model in which exosome biogenesis/release serves as a common transport 
      mechanism by which the proteins PEN1 and PEN3, otherwise resident in the plasma 
      membrane, together with membrane lipids, become stably incorporated into both 
      pathogen-induced cell wall compartments.
FAU - Meyer, Dorit
AU  - Meyer D
AD  - Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding 
      Research-Cologne, Carl-von-Linne-Weg 10, Koln, Germany.
FAU - Pajonk, Simone
AU  - Pajonk S
FAU - Micali, Cristina
AU  - Micali C
FAU - O'Connell, Richard
AU  - O'Connell R
FAU - Schulze-Lefert, Paul
AU  - Schulze-Lefert P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20081104
PL  - England
TA  - Plant J
JT  - The Plant journal : for cell and molecular biology
JID - 9207397
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (Glucans)
RN  - 0 (PEN1 protein, Arabidopsis)
RN  - 0 (Qa-SNARE Proteins)
RN  - 0 (Qb-SNARE Proteins)
RN  - 0 (Qc-SNARE Proteins)
RN  - 0 (SNAP33 protein, Arabidopsis)
RN  - 9064-51-1 (callose)
RN  - EC 2.4.1.- (Glucosyltransferases)
RN  - EC 2.4.1.34 (1,3-beta-glucan synthase)
SB  - IM
MH  - Arabidopsis/*metabolism/microbiology
MH  - Arabidopsis Proteins/*metabolism
MH  - Ascomycota/*physiology
MH  - Cell Wall/*metabolism/microbiology
MH  - Glucans/metabolism
MH  - Glucosyltransferases/metabolism
MH  - Microscopy, Confocal
MH  - Plant Epidermis/cytology/microbiology
MH  - Protein Transport
MH  - Qa-SNARE Proteins/*metabolism
MH  - Qb-SNARE Proteins/metabolism
MH  - Qc-SNARE Proteins/metabolism
MH  - Transport Vesicles/metabolism
EDAT- 2008/11/13 09:00
MHDA- 2009/03/31 09:00
CRDT- 2008/11/13 09:00
PHST- 2008/11/13 09:00 [pubmed]
PHST- 2009/03/31 09:00 [medline]
PHST- 2008/11/13 09:00 [entrez]
AID - TPJ3743 [pii]
AID - 10.1111/j.1365-313X.2008.03743.x [doi]
PST - ppublish
SO  - Plant J. 2009 Mar;57(6):986-99. doi: 10.1111/j.1365-313X.2008.03743.x. Epub 2008 
      Nov 4.