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1.
Plant J ; 62(5): 817-28, 2010 Jun 01.
Article in English | MEDLINE | ID: mdl-20230490

ABSTRACT

Through a sensitized screen for novel components of pathways regulating organ separation in Arabidopsis flowers, we have found that the leucine-rich repeat receptor-like kinase SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 (SERK1) acts as a negative regulator of abscission. Mutations in SERK1 dominantly rescue abscission in flowers without functional NEVERSHED (NEV), an ADP-ribosylation factor GTPase-activating protein required for floral organ shedding. We previously reported that the organization of the Golgi apparatus and location of the trans-Golgi network (TGN) are altered in nev mutant flowers. Disruption of SERK1 restores Golgi structure and the close association of the TGN in nev flowers, suggesting that defects in these organelles may be responsible for the block in abscission. We have also found that the abscission zones of nev serk1 flowers are enlarged compared to wild-type. A similar phenotype was previously observed in plants constitutively expressing a putative ligand required for organ separation, INFLORESCENCE DEFICIENT IN ABSCISSION (IDA), suggesting that signalling through IDA and its proposed receptors, HAESA and HAESA-LIKE2, may be deregulated in nev serk1 abscission zone cells. Our studies indicate that in addition to its previously characterized roles in stamen development and brassinosteroid perception, SERK1 plays a unique role in modulating the loss of cell adhesion that occurs during organ abscission.


Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/genetics , Flowers/growth & development , Protein Kinases/metabolism , Arabidopsis/growth & development , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Chromosome Mapping , Flowers/ultrastructure , Gene Expression Regulation, Developmental , Gene Expression Regulation, Plant , Golgi Apparatus/metabolism , Microscopy, Electron, Transmission , Mutation , Phenotype , Protein Kinases/genetics
2.
Bioorg Med Chem Lett ; 18(6): 2167-71, 2008 Mar 15.
Article in English | MEDLINE | ID: mdl-18276138

ABSTRACT

Modified adenosine derivatives may lead to the development of P2Y(12) antagonists that are potent, selective, and bind reversibly to the receptor. Analogues of 2',3'-trans-styryl acetal-N6-ureido-adenosine monophosphate were prepared by modification of the 5'-position. The resulting analogues were tested for P2Y(12) antagonism in a platelet aggregation assay.


Subject(s)
Adenosine Monophosphate/analogs & derivatives , Adenosine Monophosphate/pharmacology , Membrane Proteins/antagonists & inhibitors , Platelet Aggregation/drug effects , Purinergic P2 Receptor Antagonists , Adenosine Diphosphate/metabolism , Adenosine Monophosphate/chemical synthesis , Adenosine Triphosphate/metabolism , Chromatography, High Pressure Liquid , Humans , Magnetic Resonance Spectroscopy , Molecular Structure , Receptors, Purinergic P2Y12
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