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Special Issue "Quality Control in the Folding and Transport of Proteins Related to Human Diseases"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 June 2019).

Special Issue Editor

Prof. Dr. Tomohiko Aoe
E-Mail Website
Guest Editor
Department of Medicine, Pain Center, Chiba Medical Center, Teikyo University, Ichihara, Japan
Interests: ER stress; chaperone; BiP; vesicular transport; KDEL receptor; neurodegeneration; opioid tolerance

Special Issue Information

Dear Colleagues,

Life phenomena are a series of complicated processes, and organelles within a cell are continuously and dynamically changing. The localization of intracellular proteins represents the distribution of dynamic equilibrium at a certain time point, and the actual distribution is extensive within the cell. Peptides that become secreted proteins or membrane proteins are synthesized on the endoplasmic reticulum (ER) membrane or in the cytoplasm and inserted into the ER, having interactions with the ER molecular chaperones for folding and higher order structures. Then, they are transported to the Golgi complex, and further transported to the cell surface, where they function as membrane receptors or are externally secreted as biologically active substances. Such protein transport is carried out by vesicular transport. Besides cargo proteins, membrane components constituting intracellular organelles are also transported to both directions so that the amount of organellar membrane is balanced.

In the secretory pathway, protein quality control ensures intracellular transports of properly folded proteins to proper locations in the cell. Integrated stress responses including unfolded protein responses in the ER and heat shock responses in cytosol compensates for the accumulation of misfolded proteins due to extracellular insults such as oxidative stress and toxic substances as well as intrinsic conditions such as aging, malnutrition, and gene modifications. Beyond a certain point, however, protein folding and transports are disturbed, resulting in cellular dysfunction and cell death.

This Special Issue focuses on Quality Control in Protein Folding and Transport. Failure of this process may cause pathologic conditions. We consider insufficiencies of proteins to be folded, andwe consider machinery for protein quality control. Submissions of review articles and original studies regarding basic cellular experiments, animal models, and human diseases, which give new insights into the processes of protein quality control in the cell, are welcome. Further, submissions of review articles focusing on the latest findings in this field are encouraged.

Prof. Dr. Tomohiko Aoe
Guest Editor

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 semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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.

Keywords

  • quality control
  • proteostasis
  • ER stress
  • UPR
  • HSP
  • chaperone
  • vesicular transport
  • protein aggregation
  • conformational diseases

Published Papers (1 paper)

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Review

Open AccessReview
Pathogenic Effects of Impaired Retrieval between the Endoplasmic Reticulum and Golgi Complex
Int. J. Mol. Sci. 2019, 20(22), 5614; https://doi.org/10.3390/ijms20225614 - 09 Nov 2019
Abstract
Cellular activities, such as growth and secretion, are dependent on correct protein folding and intracellular protein transport. Injury, like ischemia, malnutrition, and invasion of toxic substances, affect the folding environment in the endoplasmic reticulum (ER). The ER senses this information, following which cells [...] Read more.
Cellular activities, such as growth and secretion, are dependent on correct protein folding and intracellular protein transport. Injury, like ischemia, malnutrition, and invasion of toxic substances, affect the folding environment in the endoplasmic reticulum (ER). The ER senses this information, following which cells adapt their response to varied situations through the unfolded protein response. Activation of the KDEL receptor, resulting from the secretion from the ER of chaperones containing the KDEL sequence, plays an important role in this adaptation. The KDEL receptor was initially shown to be necessary for the retention of KDEL sequence-containing proteins in the ER. However, it has become clear that the activated KDEL receptor also regulates bidirectional transport between the ER and the Golgi complex, as well as from the Golgi to the secretory pathway. In addition, it has been suggested that the signal for KDEL receptor activation may also affect several other cellular activities. In this review, we discuss KDEL receptor-mediated bidirectional transport and signaling and describe disease models and human diseases related to KDEL receptor dysfunction. Full article
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