Showing 1 - 10 of 12 Items
Characterizing Proteins of the Wall-Associated Kinase Signaling Pathway in Arabidopsis Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2016-01-01
Creator: Emily M King
Access: Access restricted to the Bowdoin Community
Identification of MPKs Involved in the Wall Associated Kinase Regulated Stress Response in Arabidopsis thaliana Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2013-05-01
Creator: Patrick J Lariviere
Access: Access restricted to the Bowdoin Community
ELMO, A Possible Pectin Biosynthesis Scaffold Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2023-01-01
Creator: Nuoya (Laura) Yang
Access: Access restricted to the Bowdoin Community
The Role of Protein Kinases ROG1 and SRF6 in the WAK Stress Response Pathway
Date: 2015-05-01
Creator: Jaepil E Yoon
Access: Open access
The role of the ROG1 protein in pectin perception Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2014-05-01
Creator: Divya Hoon
Access: Access restricted to the Bowdoin Community
The Roles of ROG1, REM1, and REM2 in a WAK Mediated Pectin Response Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2015-05-01
Creator: Joshua A Benton
Access: Access restricted to the Bowdoin Community
The state of cell wall pectin monitored by wall associated kinases: A model
Date: 2015-07-03
Creator: Bruce D. Kohorn
Access: Open access
- The Wall Associated Kinases (WAKs) bind to both cross-linked polymers of pectin in the plant cell wall, but have a higher affinity for smaller fragmented pectins that are generated upon pathogen attack or wounding. WAKs are required for cell expansion during normal seedling development and this involves pectin binding and a signal transduction pathway involving MPK3 and invertase induction. Alternatively WAKs bind pathogen generated pectin fragments to activate a distinct MPK6 dependent stress response. Evidence is provided for a model for how newly generated pectin fragments compete for longer pectins to alter the WAK dependent responses.
Mutation of an Arabidopsis Golgi membrane protein ELMO1 reduces cell adhesion
Date: 2021-05-01
Creator: Bruce D. Kohorn, Frances D.H. Zorensky, Jacob Dexter-Meldrum, Salem Chabout, Gregory, Mouille, Susan Kohorn
Access: Open access
- Plant growth, morphogenesis and development involve cellular adhesion, a process dependent on the composition and structure of the extracellular matrix or cell wall. Pectin in the cell wall is thought to play an essential role in adhesion, and its modification and cleavage are suggested to be highly regulated so as to change adhesive properties. To increase our understanding of plant cell adhesion, a population of ethyl methanesulfonate-mutagenized Arabidopsis were screened for hypocotyl adhesion defects using the pectin binding dye Ruthenium Red that penetrates defective but not wild-type (WT) hypocotyl cell walls. Genomic sequencing was used to identify a mutant allele of ELMO1 which encodes a 20 kDa Golgi membrane protein that has no predicted enzymatic domains. ELMO1 colocalizes with several Golgi markers and elmo1-/- plants can be rescued by an ELMO1-GFP fusion. elmo1-/- exhibits reduced mannose content relative to WT but no other cell wall changes and can be rescued to WT phenotype by mutants in ESMERALDA1, which also suppresses other adhesion mutants. elmo1 describes a previously unidentified role for the ELMO1 protein in plant cell adhesion.
The Role of the Golgi ELMO Proteins in Cell Adhesion in Arabidopsis thaliana
Date: 2021-01-01
Creator: Wesley James Hudson
Access: Open access
- Proper growth and development of plant cells is dependent upon successful cell adhesion between cells, and this is mostly mediated by pectin in the plant cell wall. Previously, the Kohorn Laboratory identified a non-enzymatic Golgi protein named ELMO1 as it is required for cell adhesion, likely acting as a scaffold for cell wall polymer synthesis. Plants with mutant ELMO1 demonstrate a weak defective cellular adhesion phenotype as well as reduced mannose content in the cell wall. ELMO1 has homologous proteins in at least 29 different vascular plants. These homologues have 2 possible deletions in their amino acid sequence, but protein modeling determined that these variations will not affect protein structure. There are 5 homologous ELMO1 proteins in Arabidopsis thaliana that have been aptly named ELMO2, ELMO3, ELMO4, ELMO5. elmo2-/-mutants revealed no mutant adhesion phenotypes, while elmo1-/-elmo2-/-double mutants revealed strong defects in adhesion. Confocal microscopy of propidium iodide-stained seedlings confirmed the lack of a phenotype for elmo2-/-mutants and showed disorganized gapping cells for the elmo1-/-elmo2-/-mutant. Additionally, while elmo2-/-did not have any change to root or hypocotyl length, elmo1-/-elmo2-/- mutants were significantly shorter in both regards. Taken together, these data support that ELMO2 and ELMO1 are partially redundant.
The Role of ELMO5 in Arabidopsis thaliana Cell Adhesion
Date: 2022-01-01
Creator: Isabel Kristina Ball
Access: Open access
- Plant cell growth and development relies on proper cellular adhesion. As the extracellular matrix serves as the area of connection between two cells, its synthesis and maintenance are essential for cellular adhesion. The middle lamella region, the layer of the extracellular matrix between two adjacent cell walls, is diffuse with the polysaccharide pectin due to its delivery by Golgi vesicles early during cell division. A Ruthenium Red screen for cellular adhesion mutants identified the family of 5 ELMO proteins that are critical for proper cellular adhesion. To further our understanding of plant cellular adhesion and pathways of pectin synthesis and modification, this work investigates ELMO5. Plants homozygous for a T-DNA insertion in ELMO5 and a new deletion mutant allele generated using CRSPR do not have a cellular adhesion phenotype, suggesting it is either not critical for cellular adhesion or is redundant with another gene. Redundancy within the ELMO family is identified through the analysis of double mutants of elmo5 and each of the other four elmo genes. Both elmo1-/- elmo5-/-and elmo4-/- elmo5-/-mutants have a visibly worse cellular adhesion defect phenotype, suggesting partial redundancy through the ELMO family. The mutants are also rescued by growth on agar, pointing to the importance of turgor pressure and osmotic potential in modulating cellular adhesion. Both ELMO4 and ELMO5 were found to localize to the Golgi using a GFP fusion, consistent with a role for ELMOs as scaffold for pectin biosynthesis.