Wheat MAPK cascade mediates SGT1 nuclear entry targeted by a stripe rust effector.

Mitogen-activated protein kinase (MAPK) cascades play a fundamental role in plant immunity by transducing external signals inside plant cells. Here, we defined a wheat MAPK cascade, composed of the mitogen-activated protein kinase kinase (MAPKK) TaMKK2 and its downstream MAPK TaMAPK6, which phosphorylates the core immune regulator TaSGT1 (suppressor of G2 allele of Skp1), resulting in enhanced nuclear entry of TaSGT1, thereby conferring resistance against the devastating wheat pathogen Puccinia striiformis f. sp.

A rust fungus effector directly binds plant pre-mRNA splice site to reprogram alternative splicing and suppress host immunity.

Alternative splicing (AS) is a crucial post-transcriptional regulatory mechanism in plant resistance. However, whether and how plant pathogens target splicing in their host remains mostly unknown. For example, although infection by Puccinia striiformis f.

A polysaccharide deacetylase from Puccinia striiformis f. sp. tritici is an important pathogenicity gene that suppresses plant immunity.

The cell wall of filamentous fungi, comprised of chitin, polysaccharide and glycoproteins, maintains the integrity of hyphae and protect them from defence responses by potential host plants. Here, we report that one polysaccharide deacetylase of Puccinia striiformis f. sp.

An effector protein of the wheat stripe rust fungus targets chloroplasts and suppresses chloroplast function.

Chloroplasts are important for photosynthesis and for plant immunity against microbial pathogens. Here we identify a haustorium-specific protein (Pst_12806) from the wheat stripe rust fungus, Puccinia striiformis f. sp.