scholarly journals Glucocorticoid Secretion Process

2020 ◽  
Author(s):  
Keyword(s):  
Secretion Process

Electron tomographic reconstruction of plastic-embedded organelles involved in the chitin secretion process

1996 ◽  
Vol 88 (1-2) ◽  
pp. 5-13 ◽  
Author(s):  
Bruce Shillito ◽  
Abraham J. Koster ◽  
Jochen Walz ◽  
Wolfgang Baumeister
Keyword(s):  
Tomographic Reconstruction ◽  
Secretion Process

scholarly journals Protein translocation: what's the problem?

2016 ◽  
Vol 44 (3) ◽  
pp. 753-759 ◽  
Author(s):  
Robin A. Corey ◽  
William J. Allen ◽  
Ian Collinson
Keyword(s):  
Molecular Mechanism ◽  
Protein Translocation ◽  
Secretion Process ◽  
Pros And Cons ◽  
Sec System ◽  
The University ◽  
Bacterial Secretion

We came together in Leeds to commemorate and celebrate the life and achievements of Prof. Stephen Baldwin. For many years we, together with Sheena Radford and Roman Tuma (colleagues also of the University of Leeds), have worked together on the problem of protein translocation through the essential and ubiquitous Sec system. Inspired and helped by Steve we may finally be making progress. My seminar described our latest hypothesis for the molecular mechanism of protein translocation, supported by results collected in Bristol and Leeds on the tractable bacterial secretion process–commonly known as the Sec system; work that will be published elsewhere. Below is a description of the alternative and contested models for protein translocation that we all have been contemplating for many years. This review will consider their pros and cons.

Involvement of a cysteine protease in the secretion process of human xylosyltransferase I

2010 ◽  
Vol 27 (3) ◽  
pp. 359-366 ◽  
Author(s):  
Claudia Pönighaus ◽  
Joachim Kuhn ◽  
Knut Kleesiek ◽  
Christian Götting
Keyword(s):  
Cysteine Protease ◽  
Secretion Process

scholarly journals Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum

2021 ◽  
Author(s):  
Chung-Ling Lu ◽  
Jacob Cain ◽  
Jon Brudvig ◽  
Steven Ortmeier ◽  
Simeon A. Boyadjiev ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Osteogenesis Imperfecta ◽  
Tissue Specificity ◽  
Bone Development ◽  
Coat Proteins ◽  
Tissue Specific ◽  
Secretion Process ◽  
Collagen Secretion ◽  
Copii Vesicle ◽  
Er Export

ABSTRACTProcollagen requires COPII coat proteins for export from the endoplasmic reticulum (ER). SEC24 is the major component of the COPII proteins that selects cargo during COPII vesicle assembly. There are four paralogs (A to D) of SEC24 in mammals, which are classified into two subgroups. Pathological mutations in SEC24D cause osteogenesis imperfecta with craniofacial dysplasia in humans and sec24d mutant fish also recapitulate this phenotypes. Consistent with the skeletal phenotypes, the secretion of collagen was severely defective in mutant fish, emphasizing the importance of SEC24D in collagen secretion. However, SEC24D patient-derived fibroblasts show only a mild secretion phenotype, suggesting tissue-specificity in the secretion process. To explore this possibility, we generated Sec24d knockout (KO) mice. Homozygous KO mice died prior to bone development. When we analyzed embryonic and extraembryonic tissues of mutant animals, we observed tissue-dependent defects of procollagen processing and ER export. The spacial patterns of these defects mirrored with SEC24B deficiency. By systematically knocking down the expression of Sec24 paralogs, we determined that, in addition to SEC24C and SEC24D, SEC24A and SEC24B also contribute to collagen secretion. In contrast, fibronectin 1 preferred either SEC24C or SEC24D. On the basis of our results, we propose that procollagen interacts with multiple SEC24 paralogs for efficient export from the ER, and that this is the basis for tissue-specific phenotypes resulting from SEC24 paralog deficiency.

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