Special Issue "Plant Cell Wall Proteins and Development"
Deadline for manuscript submissions: 31 May 2018
Dr. Elisabeth Jamet
Laboratoire de Recherche en Sciences Végétales, Université de Toulouse, CNRS, UPS, 24 Chemin de Borderouge-Auzeville, BP42617, Castanet-Tolosan 31326, France
Website | E-Mail
Interests: plant; cell wall biology; development; evolution; proteomics; post-translational modification; cell wall architecture; protein/protein; protein/polysaccharide interaction
This Special Issue, “Plant Cell Wall Proteins and Development”, will cover a selection of recent research topics in the field of cell wall biology focused on cell wall proteins and their roles during development. Experimental papers, up-to-date review articles, and commentaries will be welcome.
Plant cell walls surround cells and provide both an external protection and a mean for cell-to-cell communication. They mainly comprise polymers like polysaccharides and lignin in lignified secondary walls and a minute amount of cell wall proteins (CWPs). CWPs are major players of cell wall remodeling and signaling. Cell wall proteomics, as well as numerous genetic or biochemical studies, have revealed the high diversity of CWPs, among which proteins acting on polysaccharides, proteases, oxido-reductases, lipid-related proteins and structural proteins. CWPs may have enzymatic activities such as cutting/ligating polymers or processing/degrading proteins. They may also contribute to the supra-molecular assembly of cell walls via protein/protein or protein/polysaccharide interactions. Thanks to these biochemical activities, they contribute to the dynamincs and the functionality of cell walls. Even though many researches have already been pursued to shed light on the many roles of CWPs, many functions still remain to be discovered especially for proteins identified in cell wall proteomes with yet unknown function.Dr. Elisabeth Jamet
Prof. Christophe Dunand
Manuscript Submission Information
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access monthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.
- cell wall
- polysaccharide remodeling
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Fascinating fasciclins: a surprisingly wide-spread protein family that mediates between the cell exterior and the cell surface
Author: Georg J. Seifert
Address: University of Natural Resources and Life Science, Vienna. Department of Applied Genetics and Cell Biology; Muthgasse 18, 1190-Vienna, Austria
Abstract: The fasciclin 1 (Fas1) domain is an ancient structural motif found in extracellular proteins in all kingdoms of life and particularly abundant in plant genomes. Human Fas1 family members are associated with multiple aspects of health and disease. At the cellular level mammalian Fas1 proteins are associated with extracellular matrix structure, cell to extracellular matrix adhesion, paracrine signalling and endocytosis of proteoglycans. Mechanistically, mammalian Fas1 proteins interact with the integrin family of receptors and with both protein and carbohydrate components of the extracellular matrix. Fas1 proteins in plants have been implicated with a variety of biological functions including cellulosic and non-cellulosic cell wall structure and signalling with mechanisms of action gradually emerging. Less is known about the function of Fas1 proteins in fungi, eubacteria and archaea, however their differential presence in closely related organisms suggests their relevance for microbial life style including pathogenicity and symbiosis. The Fas1 domain accommodates multiple potential interaction surfaces enabling it to interact with both protein and carbohydrate interaction partners. The frequently observed tandem Fas1 arrangement might enable both co-operative and auto-inhibitory regulation of ligand binding. Additional protein domains and post-translational modifications are partially conserved between different evolutionary clades suggesting an ancient function of Fas1 cell surface proteins in cell to matrix adhesion. Collectively the comparison of different Fas1 proteins suggests a recurring role in the interaction between cells and their environment.