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Sorting nexin

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https://www.readbyqxmd.com/read/28778068/snx10-promotes-phagosome-maturation-in-macrophages-and-protects-mice-against-listeria-monocytogenes-infection
#1
Jun Lou, Xiawei Li, Wei Huang, Jingjing Liang, Mingzhu Zheng, Ting Xu, Jun Lyu, Dan Li, Qin Xu, Xuexiao Jin, Guotong Fu, Di Wang, Linrong Lu
Listeria monocytogenes (L. monocytogenes),which is a facultative intracellular bacterial pathogen that causes listeriosis, is widely used to study the mammalian immune response to infection. After phagocytosis by professional phagocytes, L. monocytogenes is initially contained within phagosomes, which mature into phagolysosomes, where the bacteria are degraded. Although phagocytosis and subsequent phagosome maturation is essential for the clearance of infectious microbial pathogens, the underlying regulatory mechanisms are still unclear...
July 27, 2017: Oncotarget
https://www.readbyqxmd.com/read/28771744/loss-of-sorting-nexin-5-stabilizes-internalized-growth-factor-receptors-to-promote-thyroid-cancer-progression
#2
Sumito Jitsukawa, Ryuta Kamekura, Koji Kawata, Fumie Ito, Akinori Sato, Hiroshi Matsumiya, Tomonori Nagaya, Keiji Yamashita, Terufumi Kubo, Tomoki Kikuchi, Noriyuki Sato, Tadashi Hasegawa, Hiroshi Kiyonari, Yoshiko Mukumoto, Ken-Ichi Takano, Tetsuo Himi, Shingo Ichimiya
Thyroid carcinoma is the most common endocrine malignancy and its prevalence has recently been increasing worldwide. We previously reported that the level of sorting nexin 5 (Snx5), an endosomal translocator, is preferentially decreased during the progression of well-differentiated thyroid carcinoma into poorly differentiated carcinoma. To address the functional role of Snx5 in the development and progression of thyroid carcinoma, we established Snx5-deficient (Snx5(-/-) ) mice. In comparison to wild-type (Snx5(+/+) ) mice, Snx5(-/-) mice exhibited enlarged thyroid glands that consisted of thyrocytes with large irregular-shaped vacuoles...
August 3, 2017: Journal of Pathology
https://www.readbyqxmd.com/read/28757549/updated-insight-into-the-physiological-and-pathological-roles-of-the-retromer-complex
#3
REVIEW
Yakubu Saddeeq Abubakar, Wenhui Zheng, Stefan Olsson, Jie Zhou
Retromer complexes mediate protein trafficking from the endosomes to the trans-Golgi network (TGN) or through direct recycling to the plasma membrane. In yeast, they consist of a conserved trimer of the cargo selective complex (CSC), Vps26-Vps35-Vps29 and a dimer of sorting nexins (SNXs), Vps5-Vps17. In mammals, the CSC interacts with different kinds of SNX proteins in addition to the mammalian homologues of Vps5 and Vps17, which further diversifies retromer functions. The retromer complex plays important roles in many cellular processes including restriction of invading pathogens...
July 25, 2017: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/28712807/snx16-regulates-the-recycling-of-e-cadherin-through-a-unique-mechanism-of-coordinated-membrane-and-cargo-binding
#4
Jinxin Xu, Leilei Zhang, Yinghua Ye, Yongli Shan, Chanjuan Wan, Junfeng Wang, Duanqing Pei, Xiaodong Shu, Jinsong Liu
E-Cadherin is a major component of adherens junctions on cell surfaces. SNX16 is a unique member of sorting nexins that contains a coiled-coil (CC) domain downstream of the PX domain. We report here that SNX16 regulates the recycling trafficking of E-cadherin. We solved the crystal structure of PX-CC unit of SNX16 and revealed a unique shear shaped homodimer. We identified a novel PI3P binding pocket in SNX16 that consists of both the PX and the CC domains. Surprisingly, we showed that the PPII/α2 loop, which is generally regarded as a membrane insertion loop in PX family proteins, is involved in the E-cadherin binding with SNX16...
August 1, 2017: Structure
https://www.readbyqxmd.com/read/28664153/sopb-mediated-recruitment-of-snx18-facilitates-salmonella-typhimurium-internalization-by-the-host-cell
#5
David Liebl, Xiaying Qi, Yang Zhe, Timothy C Barnett, Rohan D Teasdale
To invade epithelial cells, Salmonella enterica serovar Typhimurium (S. Typhimurium) induces macropinocytosis through the action of virulence proteins delivered across the host cell membrane via a type III secretion system. We show that after docking at the plasma membrane S. Typhimurium triggers rapid recruitment of cytosolic SNX18, a SH3-PX-BAR domain sorting nexin protein, to the bacteria-induced membrane ruffles and to the nascent Salmonella-containing vacuole. SNX18 recruitment required the inositol-phosphatase activity of the Salmonella effector SopB and an intact phosphoinositide-binding site within the PX domain of SNX18, but occurred independently of Rho-GTPases Rac1 and Cdc42 activation...
2017: Frontiers in Cellular and Infection Microbiology
https://www.readbyqxmd.com/read/28620080/the-sorting-nexin-3-retromer-pathway-regulates-the-cell-surface-localization-and-activity-of-a-wnt-activated-polycystin-channel-complex
#6
Shuang Feng, Andrew J Streets, Vasyl Nesin, Uyen Tran, Hongguang Nie, Marta Onopiuk, Oliver Wessely, Leonidas Tsiokas, Albert C M Ong
Autosomal dominant polycystic kidney disease (ADPKD) is caused by inactivating mutations in PKD1 (85%) or PKD2 (15%). The ADPKD proteins encoded by these genes, polycystin-1 (PC1) and polycystin-2 (PC2), form a plasma membrane receptor-ion channel complex. However, the mechanisms controlling the subcellular localization of PC1 and PC2 are poorly understood. Here, we investigated the involvement of the retromer complex, an ancient protein module initially discovered in yeast that regulates the retrieval, sorting, and retrograde transport of membrane receptors...
June 15, 2017: Journal of the American Society of Nephrology: JASN
https://www.readbyqxmd.com/read/28618099/epec-effector-espf-promotes-crumbs3-endocytosis-and-disrupts-epithelial-cell-polarity
#7
Rocio Tapia, Sarah E Kralicek, Gail A Hecht
Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to inject effector proteins into host intestinal epithelial cells causing diarrhoea. EPEC infection redistributes basolateral proteins β1-integrin and Na(+) /K(+) ATPase to the apical membrane of host cells. The Crumbs (Crb) polarity complex (Crb3/Pals1/Patj) is essential for epithelial cell polarisation and tight junction (TJ) assembly. Here, we demonstrate that EPEC displaces Crb3 and Pals1 from the apical membrane to the cytoplasm of cultured intestinal epithelial cells and colonocytes of infected mice...
June 15, 2017: Cellular Microbiology
https://www.readbyqxmd.com/read/28592808/snx10-gene-mutation-leading-to-osteopetrosis-with-dysfunctional-osteoclasts
#8
Eva-Lena Stattin, Petra Henning, Joakim Klar, Emma McDermott, Christina Stecksen-Blicks, Per-Erik Sandström, Therese G Kellgren, Patrik Rydén, Göran Hallmans, Torsten Lönnerholm, Adam Ameur, Miep H Helfrich, Fraser P Coxon, Niklas Dahl, Johan Wikström, Ulf H Lerner
Autosomal recessive osteopetrosis (ARO) is a heterogeneous disorder, characterized by defective osteoclastic resorption of bone that results in increased bone density. We have studied nine individuals with an intermediate form of ARO, from the county of Västerbotten in Northern Sweden. All afflicted individuals had an onset in early infancy with optic atrophy, and in four patients anemia was present at diagnosis. Tonsillar herniation, foramen magnum stenosis, and severe osteomyelitis of the jaw were common clinical features...
June 7, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28530637/cell-penetrating-peptides-selectively-targeting-smad3-inhibit-profibrotic-tgf-%C3%AE-signaling
#9
Jeong-Han Kang, Mi-Yeon Jung, Xueqian Yin, Mahefatiana Andrianifahanana, Danielle M Hernandez, Edward B Leof
TGF-β is considered a master switch in the pathogenesis of organ fibrosis. The primary mediators of this activity are the SMAD proteins, particularly SMAD3. In the current study, we have developed a cell-penetrating peptide (CPP) conjugate of the HIV TAT protein that is fused to an aminoterminal sequence of sorting nexin 9 (SNX9), which was previously shown to bind phosphorylated SMAD3 (pSMAD3). We determined that specifically preventing the nuclear import of pSMAD3 using the TAT-SNX9 peptide inhibited profibrotic TGF-β activity in murine cells and human lung fibroblasts as well as in vivo with no demonstrable toxicity...
June 30, 2017: Journal of Clinical Investigation
https://www.readbyqxmd.com/read/28498635/snx10-plays-a-critical-role-in-mmp9-secretion-via-jnk-p38-erk-signaling-pathway
#10
Chun Zhou, Ying Wang, Jin Peng, Cuixian Li, Peiqing Liu, Xiaoyan Shen
Matrix metalloproteinases (MMPs) plays a critical role in the degradation of extracellular matrix (ECM). Sorting nexin (SNX) 10 is a member of the SNX family, which functions in regulation of endosomal sorting and osteoclast activation, has been implicated to play an important role in the bone erosion of rheumatoid arthritis. In this study, we aimed to investigate the possible role of SNX10 on MMP9 secretion and the potential mechanism. By immunostaining and co-immunoprecipitation, we found that SNX10 was extensively co-localized with MMP9, indicating that SNX10 might participate in MMP9 trafficking...
May 12, 2017: Journal of Cellular Biochemistry
https://www.readbyqxmd.com/read/28477369/snx27-interactome-in-t-lymphocytes-identifies-zo-2-dynamic-redistribution-at-the-immune-synapse
#11
María Tello-Lafoz, Gonzalo Martínez-Martínez, Cristina Rodríguez-Rodríguez, Juan Pablo Albar, Morgan Huse, Severine Gharbi, Isabel Merida
T lymphocyte recognition of antigens leads to the formation of a highly organized structure termed immune synapse (IS) by analogy with the nervous synapse. Sorting nexin 27 (SNX27) controls the endosomal traffic of PDZ domain-interacting proteins, and its alteration is associated with impaired synaptic function and neurological diseases. In T lymphocytes SNX27-positive vesicles polarize to the IS, the identity of SNX27 interactors in these conditions nonetheless remains unknown. Here we used proteomics to analyze the SNX27 interactome purified from IS-forming T cells, and confirmed the conserved nature of the SNX27/WASH/retromer association in hematopoietic cells...
May 6, 2017: Traffic
https://www.readbyqxmd.com/read/28475030/characterizing-the-spatio-temporal-role-of-sorting-nexin-17-in-human-papillomavirus-trafficking
#12
Martina Bergant, Špela Peternel, David Pim, Justyna Broniarczyk, Lawrence Banks
The human papillomavirus (HPV) L2 capsid protein plays an essential role during the early stages of viral infection. Previous studies have shown that the interaction between HPV L2 and endosomal sorting nexin 17 (SNX17) is conserved across multiple PV types where it plays an essential role in infectious entry, suggesting an evolutionarily conserved pathway of PV trafficking. Here we show that the peak time of interaction between HPV-16 L2 and SNX17 is rather early, at 2 h post-infection. Interestingly, the L2-SNX17 interaction appears to be important for facilitating capsid disassembly and L1 dissociation, suggesting that L2 recruitment of SNX17 occurs prior to capsid disassembly...
April 2017: Journal of General Virology
https://www.readbyqxmd.com/read/28404745/quantitative-high-content-imaging-identifies-novel-regulators-of-neo1-trafficking-at-endosomes
#13
Lauren E Dalton, Björn D M Bean, Michael Davey, Elizabeth Conibear
P4-ATPases are a family of putative phospholipid flippases that regulate lipid membrane asymmetry, which is important for vesicle formation. Two yeast flippases, Drs2 and Neo1, have nonredundant functions in the recycling of the synaptobrevin-like v-SNARE Snc1 from early endosomes. Drs2 activity is needed to form vesicles and regulate its own trafficking, suggesting that flippase activity and localization are linked. However, the role of Neo1 in endosomal recycling is not well characterized. To identify novel regulators of Neo1 trafficking and activity at endosomes, we first identified mutants with impaired recycling of a Snc1-based reporter and subsequently used high-content microscopy to classify these mutants based on the localization of Neo1 or its binding partners, Mon2 and Dop1...
June 1, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28381192/downregulation-of-sorting-nexin-10-is-associated-with-overexpression-of-mir-30d-during-liver-cancer-progression-in-rats
#14
Nancy Cervantes-Anaya, Alberto Ponciano-Gómez, Guadalupe Soledad López-Álvarez, Christian Gonzalez-Reyes, Sergio Hernández-Garcia, María Asunción Cabañas-Cortes, José Efraín Garrido-Guerrero, Saúl Villa-Treviño
As of 2012, liver cancer was the second leading cause of death worldwide, and hepatocellular carcinoma is the most common primary cancer of the liver. The identification of molecules that might be molecular markers or therapeutic targets is urgently needed to improve clinical management. Based on a microarray analysis performed in our laboratory, we selected six genes-namely, ANXA2, DYNLT1, PFKP, PLA2G7, KRT19, and SNX10-as candidates for validation as tumor markers of liver cancer in a rat model. Their patterns of overexpression in preneoplastic lesions and established tumors at 10 different time points between 24 h and 18 months were analyzed to identify putative tumor markers for further studies...
April 2017: Tumour Biology: the Journal of the International Society for Oncodevelopmental Biology and Medicine
https://www.readbyqxmd.com/read/28266622/sorting-nexin-9-facilitates-podocin-endocytosis-in-the-injured-podocyte
#15
Yu Sasaki, Teruo Hidaka, Takashi Ueno, Miyuki Akiba-Takagi, Juan Alejandro Oliva Trejo, Takuto Seki, Yoshiko Nagai-Hosoe, Eriko Tanaka, Satoshi Horikoshi, Yasuhiko Tomino, Yusuke Suzuki, Katsuhiko Asanuma
The irreversibility of glomerulosclerotic changes depends on the degree of podocyte injury. We have previously demonstrated the endocytic translocation of podocin to the subcellular area in severely injured podocytes and found that this process is the primary disease trigger. Here we identified the protein sorting nexin 9 (SNX9) as a novel facilitator of podocin endocytosis in a yeast two-hybrid analysis. SNX9 is involved in clathrin-mediated endocytosis, actin rearrangement and vesicle transport regulation...
March 7, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28252385/chlamydia-interfere-with-an-interaction-between-the-mannose-6-phosphate-receptor-and-sorting-nexins-to-counteract-host-restriction
#16
Cherilyn A Elwell, Nadine Czudnochowski, John von Dollen, Jeffrey R Johnson, Rachel Nakagawa, Kathleen Mirrashidi, Nevan J Krogan, Joanne N Engel, Oren S Rosenberg
Chlamydia trachomatis is an obligate intracellular pathogen that resides in a membrane-bound compartment, the inclusion. The bacteria secrete a unique class of proteins, Incs, which insert into the inclusion membrane and modulate the host-bacterium interface. We previously reported that IncE binds specifically to the Sorting Nexin 5 Phox domain (SNX5-PX) and disrupts retromer trafficking. Here, we present the crystal structure of the SNX5-PX:IncE complex, showing IncE bound to a unique and highly conserved hydrophobic groove on SNX5...
March 2, 2017: ELife
https://www.readbyqxmd.com/read/28235896/pathogenic-huntington-alters-bmp-signaling-and-synaptic-growth-through-local-disruptions-of-endosomal-compartments
#17
Yulia Akbergenova, J Troy Littleton
Huntington's disease (HD) is a neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) stretch within the Huntingtin (Htt) protein. Pathogenic Htt disrupts multiple neuronal processes, including gene expression, axonal trafficking, proteasome and mitochondrial activity, and intracellular vesicle trafficking. However, the primary pathogenic mechanism and subcellular site of action for mutant Htt are still unclear. Using a Drosophila HD model, we found that pathogenic Htt expression leads to a profound overgrowth of synaptic connections that correlates directly with the levels of Htt at nerve terminals...
March 22, 2017: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/28226239/structural-basis-for-the-hijacking-of-endosomal-sorting-nexin-proteins-by-chlamydia-trachomatis
#18
Blessy Paul, Hyun Sung Kim, Markus C Kerr, Wilhelmina M Huston, Rohan D Teasdale, Brett M Collins
During infection chlamydial pathogens form an intracellular membrane-bound replicative niche termed the inclusion, which is enriched with bacterial transmembrane proteins called Incs. Incs bind and manipulate host cell proteins to promote inclusion expansion and provide camouflage against innate immune responses. Sorting nexin (SNX) proteins that normally function in endosomal membrane trafficking are a major class of inclusion-associated host proteins, and are recruited by IncE/CT116. Crystal structures of the SNX5 phox-homology (PX) domain in complex with IncE define the precise molecular basis for these interactions...
February 22, 2017: ELife
https://www.readbyqxmd.com/read/28179995/caspase-mediated-proteolysis-of-the-sorting-nexin-2-disrupts-retromer-assembly-and-potentiates-met-hepatocyte-growth-factor-receptor-signaling
#19
Catherine M Duclos, Audrey Champagne, Julie C Carrier, Caroline Saucier, Christine L Lavoie, Jean-Bernard Denault
The unfolding of apoptosis involves the cleavage of hundreds of proteins by the caspase family of cysteinyl peptidases. Among those substrates are proteins involved in intracellular vesicle trafficking with a net outcome of shutting down the crucial processes governing protein transport to organelles and to the plasma membrane. However, because of the intertwining of receptor trafficking and signaling, cleavage of specific proteins may lead to unintended consequences. Here we show that in apoptosis, sorting nexin 1 and 2 (SNX1 and SNX2), two proteins involved in endosomal sorting, are cleaved by initiator caspases and also by executioner caspase-6 in the case of SNX2...
2017: Cell Death Discovery
https://www.readbyqxmd.com/read/28125336/new-insights-into-mechanisms-of-nuclear-translocation-of-g-protein-coupled-receptors
#20
Vikrant K Bhosle, José Carlos Rivera, Sylvain Chemtob
The G-protein coupled receptor (GPCR) signaling was long believed to involve activation of receptor exclusively at the cell surface, followed by its binding to heterotrimeric G-proteins and arrestins to trigger various intracellular signaling cascades, and termination of signaling by internalization of the receptor. It is now accepted that many GPCRs continue to signal after internalization in the endosomes. Since the breakthrough discoveries of nuclear binding sites for their ligands in 1980s, several GPCRs have been detected at cell nuclei...
January 26, 2017: Small GTPases
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