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Cowden Syndrome
Published in Dongyou Liu, Handbook of Tumor Syndromes, 2020
Located on in the short (p) arm of chromosome 20 at position 11.23 (i.e., 20p11.23), the SEC23B gene encodes a component of coat protein complex II (COPII), which is involved in the formation of vesicles (so-called endoplasmic reticulum [ER]) for transportation of proteins and other materials within cells. Mutations in the SEC23B gene are identified in 2% of all Cowden syndrome cases and may be also responsible for producing unusually shaped erythroblasts with extra nuclei that cannot mature into functional red blood cells, leading to congenital dyserythropoietic anemia type II, enlarged liver and spleen (hepatosplenomegaly), and an abnormal buildup of iron [14].
Golgi apparatus regulation of differentiation
Published in C. Yan Cheng, Spermatogenesis, 2018
Louis Hermo, Regiana L. Oliveira, Charles E. Smith, Catherine E. Au, John J. M. Bergeron
Sec23 is a component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum. Mutations affecting SEC23IP, a phospholipaseA1-like protein that interacts with Sec23, also cause male subfertility by interfering with acrosome biogenesis and leading to round-headed spermatozoa.166
Cholix protein domain I functions as a carrier element for efficient apical to basal epithelial transcytosis
Published in Tissue Barriers, 2020
Alistair Taverner, Julia MacKay, Floriane Laurent, Tom Hunter, Keyi Liu, Khushdeep Mangat, Lisa Song, Elbert Seto, Sally Postlethwaite, Aatif Alam, Apurva Chandalia, Minji Seung, Mazi Saberi, Weijun Feng, Randall J. Mrsny
COPI and COPII coating machineries can be used as hallmarks for the movement of vesicles between the endoplasmic reticulum (ER), ER exit sites, ER-to-Golgi intermediate compartment (ERGIC), Golgi complex, and TGN that provide routing for newly synthesized secretory proteins destined to the secretory and endolysosomal systems as well as directing the fate of internalized proteins following endocytosis at the plasma membrane.21 In untreated intestinal tissues, COPI was observed to be adjacent to the apical plasma membrane and distributed in the apical vesicular region of rat enterocytes (Figure 5a). Remarkably, by 15 min post-ILI of Chx266-hGH, COPI was observed almost exclusively in the supranuclear region of enterocytes (Figure 5b). A striking re-organization for COPII was also observed: COPII was localized primarily to a supranuclear region and in the basal vesicular region of untreated enterocytes (Figure 5c) but moved to a predominantly apical vesicular region distribution with a much reduced distribution in the basal vesicular region by 15-min post-ILI of Chx266-hGH (Figure 5d). These results suggested that Chx transcytosis coincided with striking reorganizations of COPI and COPII distribution enterocytes. ILI of hGH alone (not conjoined to Chx266) did not affect COPI or COPII cellular distribution (data not shown).
Inhibition of anti-viral responses in intestinal epithelial cells by epigenetic modifying drugs is mediated by a reduction in viral pattern recognition receptor expression and activity
Published in Immunopharmacology and Immunotoxicology, 2019
Conor Hennessy, Sarah O’Connell, Laurence J. Egan, Declan P. McKernan
While we provided evidence of IRF8 expression correlating with changes in TLR3, there are other potential regulators that we didn’t investigate such as p53, which can be a positively regulator of TLR3 expression. Previous publications by Taura and colleagues have shown that induction of TLR3 expression is absent in p53 knockout cells and in addition chemotherapeutic drugs (that induce p53 expression) increase the sensitivity of intestinal epithelial cells to death by the TLR3 ligand Poly I:C by increasing TLR3 expression [44,45]. Another possible explanation for our observations could be altered trafficking of the TLR3 receptor. Intracellular TLRs undergo trafficking via the endoplasmic reticulum to the Golgi apparatus, involving several regulatory steps. Unc93b1 is a trafficking chaperone that is involved in the ER export and partitioning of TLRs into endolysosomes [46,47]. Previous studies have shown that nonfunctioning variants of this Unc93b1 protein have resulted in the failure of ER export of TLRs as well as the loss of TLR signaling [48,49]. Other recent studies have uncovered another trafficking protein involved in TLR trafficking, LRRC59. It was shown to have a role in loading TLRs into coat protein complex (COPII) vesicles, which are involved in transporting proteins form the ER to the Golgi apparatus [50]. Epigenetic regulation of these chaperone proteins could result in a nonfunctional TLR3 response, despite adequate expression.
Novel therapeutic strategies for stroke: The role of autophagy
Published in Critical Reviews in Clinical Laboratory Sciences, 2019
Seyed Fazel Nabavi, Antoni Sureda, Ana Sanches-Silva, Kasi Pandima Devi, Touqeer Ahmed, Momina Shahid, Eduardo Sobarzo-Sánchez, Marco Dacrema, Maria Daglia, Nady Braidy, Rosa Anna Vacca, Ioana Berindan-Neagoe, Diana Gulei, Davide Barreca, Maciej Banach, Seyed Mohammad Nabavi, Ahmad Reza Dehpour, Samira Shirooie
In yeast, the transition from initiation to nucleation is determined by the intervention of scaffold proteins, such as transport protein particle III (TRAPPIII) and a Rab1 family GTPase called Ypt1/RAB1 in mammals. Their task is to deliver the Atg9 vesicle and coat protein complex II (COPII) to induce the next phase of autophagy [37,38]. In mammals, this event drives the formation of the PI3K complex III, which consists of UV irradiation resistance-associated tumor suppressor gene (UVRAG/Vsp38 in yeast), Beclin-1 (BECN-1/Vps30-Atg6 in yeast), and myristylated kinase (VPS15, p150/Vps15 in yeast). This complex allows the phosphorylation of its catalytic subunit VPS34, inducing the production of phospatidylinositol-3-phospate (PtdIns3P), which plays a substantial role in the elongation of the phagophore and the recruitment of additional Atg proteins to the phagophore [30,39].