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Salicylic acid interferes with clathrin-mediated endocytic protein trafficking.


ABSTRACT: Removal of cargos from the cell surface via endocytosis is an efficient mechanism to regulate activities of plasma membrane (PM)-resident proteins, such as receptors or transporters. Salicylic acid (SA) is an important plant hormone that is traditionally associated with pathogen defense. Here, we describe an unanticipated effect of SA on subcellular endocytic cycling of proteins. Both exogenous treatments and endogenously enhanced SA levels repressed endocytosis of different PM proteins. The SA effect on endocytosis did not involve transcription or known components of the SA signaling pathway for transcriptional regulation. SA likely targets an endocytic mechanism that involves the coat protein clathrin, because SA interfered with the clathrin incidence at the PM and clathrin-deficient mutants were less sensitive to the impact of SA on the auxin distribution and root bending during the gravitropic response. By contrast, SA did not affect the ligand-induced endocytosis of the flagellin sensing2 (FLS2) receptor during pathogen responses. Our data suggest that the established SA impact on transcription in plant immunity and the nontranscriptional effect of SA on clathrin-mediated endocytosis are independent mechanisms by which SA regulates distinct aspects of plant physiology.

SUBMITTER: Du Y 

PROVIDER: S-EPMC3651428 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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Salicylic acid interferes with clathrin-mediated endocytic protein trafficking.

Du Yunlong Y   Tejos Ricardo R   Beck Martina M   Himschoot Ellie E   Li Hongjiang H   Robatzek Silke S   Vanneste Steffen S   Friml Jirí J  

Proceedings of the National Academy of Sciences of the United States of America 20130423 19


Removal of cargos from the cell surface via endocytosis is an efficient mechanism to regulate activities of plasma membrane (PM)-resident proteins, such as receptors or transporters. Salicylic acid (SA) is an important plant hormone that is traditionally associated with pathogen defense. Here, we describe an unanticipated effect of SA on subcellular endocytic cycling of proteins. Both exogenous treatments and endogenously enhanced SA levels repressed endocytosis of different PM proteins. The SA  ...[more]

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