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Sorting nexin

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https://www.readbyqxmd.com/read/28266622/sorting-nexin-9-facilitates-podocin-endocytosis-in-the-injured-podocyte
#1
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
#2
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
#3
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 directly correlates with the levels of Htt at nerve terminals...
February 24, 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
#4
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
#5
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
#6
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
https://www.readbyqxmd.com/read/28109317/sorting-nexin-4-regulates-%C3%AE-amyloid-production-by-modulating-%C3%AE-site-activating-cleavage-enzyme-1
#7
Na-Young Kim, Mi-Hyang Cho, Se-Hoon Won, Hoe-Jin Kang, Seung-Yong Yoon, Dong-Hou Kim
BACKGROUND: Amyloid precursor protein (APP) is cleaved by β-site amyloid precursor protein-cleaving enzyme 1 (BACE1) to produce β-amyloid (Aβ), a critical pathogenic peptide in Alzheimer's disease (AD). Aβ generation can be affected by the intracellular trafficking of APP or its related secretases, which is thus important to understanding its pathological alterations. Although sorting nexin (SNX) family proteins regulate this trafficking, the relevance and role of sorting nexin-4 (SNX4) regarding AD has not been studied yet...
January 21, 2017: Alzheimer's Research & Therapy
https://www.readbyqxmd.com/read/28100638/retromer-driven-membrane-tubulation-separates-endosomal-recycling-from-rab7-ypt7-dependent-fusion
#8
Latha Kallur Purushothaman, Henning Arlt, Anne Kuhlee, Stefan Raunser, Christian Ungermann
Endosomes are the major protein sorting hubs of the endocytic pathway. They sort proteins destined for degradation into internal vesicles, while in parallel recycling receptors via tubular carriers back to the Golgi. Tubule formation depends on the Rab7/Ypt7-interacting retromer complex, consisting of the sorting nexin dimer (SNX-BAR) and the trimeric cargo selection complex (CSC). Fusion of mature endosomes with the lysosome-like vacuole also requires Rab7/Ypt7. Here, we now solved a major problem in understanding this dual function of endosomal Rab7/Ypt7 using a fully reconstituted system, including purified, full-length yeast SNX-BAR and CSC, whose overall structure we present...
January 18, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28053230/snx-1-and-rme-8-oppose-the-assembly-of-hgrs-1-escrt-0-degradative-microdomains-on-endosomes
#9
Anne Norris, Prasad Tammineni, Simon Wang, Julianne Gerdes, Alexandra Murr, Kelvin Y Kwan, Qian Cai, Barth D Grant
After endocytosis, transmembrane cargo reaches endosomes, where it encounters complexes dedicated to opposing functions: recycling and degradation. Microdomains containing endosomal sorting complexes required for transport (ESCRT)-0 component Hrs [hepatocyte growth factor-regulated tyrosine kinase substrate (HGRS-1) in Caenorhabditis elegans] mediate cargo degradation, concentrating ubiquitinated cargo and organizing the activities of ESCRT. At the same time, retromer associated sorting nexin one (SNX-1) and its binding partner, J-domain protein RME-8, sort cargo away from degradation, promoting cargo recycling to the Golgi...
January 17, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27989654/endocytosis-metastasis-and-beyond-multiple-facets-of-snx9
#10
REVIEW
Nawal Bendris, Sandra L Schmid
Sorting nexin (SNX)9 was first discovered as an endocytic accessory protein involved in clathrin-mediated endocytosis. However, recent data suggest that SNX9 is a multifunctional scaffold that coordinates membrane trafficking and remodeling with changes in actin dynamics to affect diverse cellular processes. Here, we review the accumulated knowledge on SNX9 with an emphasis on its recently identified roles in clathrin-independent endocytic pathways, cell invasion, and cell division, which have implications for SNX9 function in human disease, including cancer...
March 2017: Trends in Cell Biology
https://www.readbyqxmd.com/read/27889239/structural-mechanism-for-cargo-recognition-by-the-retromer-complex
#11
María Lucas, David C Gershlick, Ander Vidaurrazaga, Adriana L Rojas, Juan S Bonifacino, Aitor Hierro
Retromer is a multi-protein complex that recycles transmembrane cargo from endosomes to the trans-Golgi network and the plasma membrane. Defects in retromer impair various cellular processes and underlie some forms of Alzheimer's disease and Parkinson's disease. Although retromer was discovered over 15 years ago, the mechanisms for cargo recognition and recruitment to endosomes have remained elusive. Here, we present an X-ray crystallographic analysis of a four-component complex comprising the VPS26 and VPS35 subunits of retromer, the sorting nexin SNX3, and a recycling signal from the divalent cation transporter DMT1-II...
December 1, 2016: Cell
https://www.readbyqxmd.com/read/27889227/gpcr-signaling-and-trafficking-the-long-and-short-of-it
#12
REVIEW
Nathan J Pavlos, Peter A Friedman
Emerging findings disclose unexpected components of G protein-coupled receptor (GPCR) signaling and cell biology. Select GPCRs exhibit classical signaling, that is restricted to cell membranes, as well as newly described persistent signaling that depends on internalization of the GPCR bound to β-arrestins. Termination of non-canonical endosomal signaling requires intraluminal acidification and sophisticated protein trafficking machineries. Recent studies reveal the structural determinants of the trafficking chaperones...
March 2017: Trends in Endocrinology and Metabolism: TEM
https://www.readbyqxmd.com/read/27883263/cargo-selectivity-of-yeast-sorting-nexins
#13
Björn D M Bean, Michael Davey, Elizabeth Conibear
Sorting nexins are PX domain-containing proteins that bind phospholipids and often act in membrane trafficking where they help to select cargo. However, the functions and cargo specificities of many sorting nexins are unknown. Here, a high-throughput imaging screen was used to identify new sorting nexin cargo in the yeast Saccharomyces cerevisiae. Deletions of 9 different sorting nexins were screened for mislocalization of a set of green fluorescent protein (GFP)-tagged membrane proteins found at the plasma membrane, Golgi or endosomes...
February 2017: Traffic
https://www.readbyqxmd.com/read/27827364/structural-and-mechanistic-insights-into-regulation-of-the-retromer-coat-by-tbc1d5
#14
Da Jia, Jin-San Zhang, Fang Li, Jing Wang, Zhihui Deng, Mark A White, Douglas G Osborne, Christine Phillips-Krawczak, Timothy S Gomez, Haiying Li, Amika Singla, Ezra Burstein, Daniel D Billadeau, Michael K Rosen
Retromer is a membrane coat complex that is recruited to endosomes by the small GTPase Rab7 and sorting nexin 3. The timing of this interaction and consequent endosomal dynamics are thought to be regulated by the guanine nucleotide cycle of Rab7. Here we demonstrate that TBC1d5, a GTPase-activating protein (GAP) for Rab7, is a high-affinity ligand of the retromer cargo selective complex VPS26/VPS29/VPS35. The crystal structure of the TBC1d5 GAP domain bound to VPS29 and complementary biochemical and cellular data show that a loop from TBC1d5 binds to a conserved hydrophobic pocket on VPS29 opposite the VPS29-VPS35 interface...
November 9, 2016: Nature Communications
https://www.readbyqxmd.com/read/27778231/identification-of-potential-predictive-markers-of-dexamethasone-resistance-in-childhood-acute-lymphoblastic-leukemia
#15
Nasrin Dehghan-Nayeri, Mostafa Rezaei-Tavirani, Mir Davood Omrani, Ahmad Gharehbaghian, Kourosh Goudarzi Pour, Peyman Eshghi
Response to dexamethasone (DEXA), as a hallmark drug in the treatment of childhood acute lymphoblastic leukemia (ALL), is one of the pivotal prognostic factors in the prediction of outcome in ALL. Identification of predictive markers of chemoresistance is beneficial to selecting of the best therapeutic protocol with the lowest effect adverse. Hence, we aimed to find drug targets using the 2DE/MS proteomics study of a DEXA-resistant cell line (REH) as a model for poor DEXA responding patients before and after drug treatment...
October 24, 2016: Journal of Cell Communication and Signaling
https://www.readbyqxmd.com/read/27766425/reduced-expression-of-setd2-and-snx9-proteins-in-chemically-induced-mammary-tumorigenesis-in-wistar-rats-a-prognostic-histological-and-proteomic-study
#16
Ishfaq Ahmad Ganaie, Samar Husain Naqvi, Swatantra Kumar Jain, Saima Wajid
Breast cancer is a major global health concern, appealing for precise prognostic approaches. Thus, the need is to have studies focusing on the identification and recognition of preliminary events leading to the disease. The present study reports the tracing of precancerous progression and serum proteomic analysis in a breast cancer model developed as a result of 7,12-dimethylbenz[a]anthracene (DMBA) administration. Mammary gland histological changes of prime importance were examined by histopathology, and immunohistochemical analysis with Ki-67 was performed to monitor enhanced cell proliferation, right from the onset of hyperplasia till neoplasia...
October 20, 2016: Protoplasma
https://www.readbyqxmd.com/read/27761583/several-adaptor-proteins-promote-intracellular-localisation-of-the-transporter-mrp4-abcc4-in-platelets-and-haematopoietic-cells
#17
Yvonne Schaletzki, Marie-Luise Kromrey, Susanne Bröderdorf, Elke Hammer, Markus Grube, Paul Hagen, Sonja Sucic, Michael Freissmuth, Uwe Völker, Andreas Greinacher, Bernhard H Rauch, Heyo K Kroemer, Gabriele Jedlitschky
The multidrug resistance protein 4 (MRP4/ABCC4) has been identified as an important transporter for signalling molecules including cyclic nucleotides and several lipid mediators in platelets and may thus represent a novel target to interfere with platelet function. Besides its localisation in the plasma membrane, MRP4 has been also detected in the membrane of dense granules in resting platelets. In polarised cells it is localised at the basolateral or apical plasma membrane. To date, the mechanism of MRP4 trafficking has not been elucidated; protein interactions may regulate both the localisation and function of this transporter...
October 20, 2016: Thrombosis and Haemostasis
https://www.readbyqxmd.com/read/27725825/differential-gene-expression-and-protein-phosphorylation-as-factors-regulating-the-state-of-the-arabidopsis-snx1-protein-complexes-in-response-to-environmental-stimuli
#18
Tzvetina Brumbarova, Rumen Ivanov
Endosomal recycling of plasma membrane proteins contributes significantly to the regulation of cellular transport and signaling processes. Members of the Arabidopsis (Arabidopsis thaliana) SORTING NEXIN (SNX) protein family were shown to mediate the endosomal retrieval of transporter proteins in response to external challenges. Our aim is to understand the possible ways through which external stimuli influence the activity of SNX1 in the root. Several proteins are known to contribute to the function of SNX1 through direct protein-protein interaction...
2016: Frontiers in Plant Science
https://www.readbyqxmd.com/read/27649450/interaction-of-the-human-papillomavirus-e6-oncoprotein-with-sorting-nexin-27-modulates-endocytic-cargo-transport-pathways
#19
Ketaki Ganti, Paola Massimi, Joaquin Manzo-Merino, Vjekoslav Tomaić, David Pim, Martin P Playford, Marcela Lizano, Sally Roberts, Christian Kranjec, John Doorbar, Lawrence Banks
A subset of high-risk Human Papillomaviruses (HPVs) are the causative agents of a large number of human cancers, of which cervical is the most common. Two viral oncoproteins, E6 and E7, contribute directly towards the development and maintenance of malignancy. A characteristic feature of the E6 oncoproteins from cancer-causing HPV types is the presence of a PDZ binding motif (PBM) at its C-terminus, which confers interaction with cellular proteins harbouring PDZ domains. Here we show that this motif allows E6 interaction with Sorting Nexin 27 (SNX27), an essential component of endosomal recycling pathways...
September 2016: PLoS Pathogens
https://www.readbyqxmd.com/read/27646272/distinct-g-protein-coupled-receptor-recycling-pathways-allow-spatial-control-of-downstream-g-protein-signaling
#20
Shanna Lynn Bowman, Daniel John Shiwarski, Manojkumar A Puthenveedu
G protein-coupled receptors (GPCRs) are recycled via a sequence-dependent pathway that is spatially and biochemically distinct from bulk recycling. Why there are two distinct recycling pathways from the endosome is a fundamental question in cell biology. In this study, we show that the separation of these two pathways is essential for normal spatial encoding of GPCR signaling. The prototypical β-2 adrenergic receptor (B2AR) activates Gα stimulatory protein (Gαs) on the endosome exclusively in sequence-dependent recycling tubules marked by actin/sorting nexin/retromer tubular (ASRT) microdomains...
September 26, 2016: Journal of Cell Biology
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