Special Issue "Protein Ubiquitination"
A special issue of Cells (ISSN 2073-4409).
Deadline for manuscript submissions: 15 March 2014
Prof. Dr. Hanjo Hellmann
Plant Stress Physiology, School of Biological Sciences, Washington State University, Pullman, WA, USA
Phone: +1 509 335 2762
Interests: ubiquitin proteasome pathway; E3 ligases; stress physiology; vitamin B6 metabolism
Since the discovery of the ubiquitin proteasome pathway in the late 1970’s, tremendous progress has been accomplished in understanding its mechanism, and revealing its conserved nature across the different eukaryotic kingdoms. The pathway functions as one of the major regulatory switches in the cell and affects a broad range of processes such as cell division, transcriptional activity, stress responses and transport processes. Although the pathway is often mainly connected with degradation of ubiquitylated proteins, it also has major impact in controlling activity and subcellular localization of proteins, independently of proteolysis.
This Special Issue will provide an Open Access opportunity to publish research work and review articles related to the ubiquitin proteasome pathway, and to offer comprehensive new insights into current developments of this exciting and important research field.
Dr. Hanjo Hellmann
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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed Open Access quarterly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. For the first couple of issues the Article Processing Charge (APC) will be waived for well-prepared manuscripts. English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.
- ubiquitin chain
- 26S proteasome
- protein stability
- protein localization
- E3 ligases
- cellular regulation
- signal transduction
Cells 2013, 2(4), 732-750; doi:10.3390/cells2040732
Received: 7 October 2013; in revised form: 12 November 2013 / Accepted: 29 November 2013 / Published: 5 December 2013| Download PDF Full-text (506 KB) | Download XML Full-text
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: The Ubiquitin-Proteasome System in Viral Infection
Authors: Arianna Calistri 1, Francesca Spanevello 1, Cristina Parolin 2, Giorgio Palù 1,*
Affiliations: 1 Department of Molecular Medicine, University of Padova, Via Aristide Gabelli 63, Padova 35121, Italy
2 Department of Biology, University of Padova, Via Ugo Bassi 58/B, 35121 Padova, Italy; * E-Mail: firstname.lastname@example.org
Abstract: The best characterized outcome of ubiquitination is the degradation of proteins linked to multi-ubiquitin (Ub) chains through the proteasome. On the other hand, mono-ubiquitination of proteins is a signal for their internalization from the cell membrane and for their sorting from the endocytic pathway into the multivesicular body (MVB)/late endosomes. The cellular ubiquitination pathway is clearly involved in several steps of viral life cycle. We contributed to the discovery that the sorting function of ubiquitinatin and the MVB biogenesis pathway are relevant for viral release from infected cells. In addition, ubiquitination of cellular proteins mediated by viral encoded Ub ligases (E3) or by cellular E3 enzymes modified by viral factors enables viruses to overcome different intracellular defence mechanisms. In this review we will discussed the most updated evidence on the role played by the ubiquitin-proteasome system in viral replication with a special focus on viral budding and on viral escape from innate immunity.
Type of Paper: Review
Title: Ubiquitination Controls Morphology and Functions of Sperm Organelles
Author: Nobuhiro Nakamura
Affiliation: Nakamura Lab, Department of Biological Sciences, Tokyo Institute of Technology, 4259-B-13 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan; E-Mail: email@example.com
Abstract: Now we know that ubiquitination has diverse cellular functions in eukaryotes. The molecular mechanism and physiological significance of ubiquitin-mediated processes have been extensively studied in yeast and mammalian somatic cells. However, an increasing number of studies have emphasized the importance of ubiquitination in gamategenesis and fertilization. This review will focus on the emerging roles of ubiquitination in biogenesis, functions and stability of sperm organelles.
Last update: 12 August 2013