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Lectin and ER and channel protein

Dong-Yun Han, Bo-Jhih Guan, Ya-Juan Wang, Maria Hatzoglou, Ting-Wei Mu
Gamma-aminobutyric acid type A (GABAA) receptors are the primary inhibitory ion channels in the mammalian central nervous system and play an essential role in regulating inhibition-excitation balance in neural circuits. The α1 subunit harboring the D219N mutation of GABAA receptors was reported to be retained in the endoplasmic reticulum (ER) and traffic inefficiently to the plasma membrane, leading to a loss of function of α1(D219N) subunits and thus idiopathic generalized epilepsy (IGE). We present the use of small molecule proteostasis regulators to enhance the forward trafficking of α1(D219N) subunits to restore their function...
September 18, 2015: ACS Chemical Biology
Peter O Bauer, Roman Hudec, Anand Goswami, Masaru Kurosawa, Gen Matsumoto, Katsuhiko Mikoshiba, Nobuyuki Nukina
BACKGROUND: Huntington's Disease (HD) is a fatal hereditary neurodegenerative disease caused by the accumulation of mutant huntingtin protein (Htt) containing an expanded polyglutamine (polyQ) tract. Activation of the channel responsible for the inositol-induced Ca²⁺ release from ensoplasmic reticulum (ER), was found to contribute substantially to neurodegeneration in HD. Importantly, chemical and genetic inhibition of inositol 1,4,5-trisphosphate (IP3) receptor type 1 (IP3R1) has been shown to reduce mutant Htt aggregation...
2012: Molecular Neurodegeneration
Hao Zhang, Eric Peatman, Hong Liu, Tingting Feng, Liqiao Chen, Zhanjiang Liu
L-type lectins have a leguminous lectin domain and can bind to high-mannose type oligosaccharides. In the secretory pathway, L-type lectins play crucial roles in selective protein trafficking, sorting and targeting. Three L-type lectins were cloned in the channel catfish, Ictalurus punctatus, the 53 kDa endoplasmic reticulum ER-Golgi intermediate compartment protein (ERGIC-53), the vesicular integral protein of 36 kDa (VIP36) and VIP36-like. Phylogenetic analysis indicated that the catfish genes are orthologous to their counterparts in other species...
April 2012: Fish & Shellfish Immunology
Masatoshi Hagiwara, Kazuhiro Nagata
SIGNIFICANCE: Nascent polypeptides entering the endoplasmic reticulum (ER) are co- and post-translationally modified by N-glycosylation and the oxidation/isomerization of cysteine residues followed by folding with the aid of molecular chaperones. Only properly folded proteins reach their final destination. The oxidative environment in the ER enables ER-resident oxidoreductases to facilitate disulfide bond formation, which stabilizes protein structures. ER oxidoreductases involve in both the productive folding of newly synthesized proteins and ER-associated degradation (ERAD) of misfolded proteins...
May 15, 2012: Antioxidants & Redox Signaling
Timothy Ryan, Parveen Sharma, Alex Ignatchenko, David H MacLennan, Thomas Kislinger, Anthony O Gramolini
The ryanodine receptor type 1 (RyR1) is a homotetrameric Ca(2+) release channel located in the sarcoplasmic reticulum of skeletal muscle where it plays a role in the initiation of skeletal muscle contraction. A soluble, 6×-histidine affinity-tagged cytosolic fragment of RyR1 (amino acids 1-4243) was expressed in HEK-293 cells, and metal affinity chromatography under native conditions was used to purify the peptide together with interacting proteins. When analyzed by gel-free liquid chromatography mass spectrometry (LC-MS), 703 proteins were identified under all conditions...
May 13, 2011: Journal of Biological Chemistry
Jun Hoseki, Ryo Ushioda, Kazuhiro Nagata
The folding of secretory and membrane proteins takes place in the endoplasmic reticulum (ER). The quality of the proteins folded in the ER is carefully monitored by an ER quality control mechanism that allows only correctly folded proteins to be transported to their final destination, and misfolded or unassembled proteins to be retained in the ER and subsequently degraded in a process termed 'ER-associated degradation' (ERAD). The ERAD pathway is conserved from yeast to mammals, and plays an essential role in the maintenance of ER homeostasis, as well as in the prevention of various diseases that arise from the accumulation of aberrant proteins in the ER...
January 2010: Journal of Biochemistry
Takuya Sugahara, Tomoaki Koga, Keiko Ueno-Shuto, Tsuyoshi Shuto, Eriko Watanabe, Ai Maekawa, Kenichiro Kitamura, Kimio Tomita, Ai Mizuno, Takashi Sato, Mary Ann Suico, Hirofumi Kai
Epithelial sodium channel (ENaC) is a heteromultimeric Na(+) channel at the apical membrane in the kidney, colon, and lung. Because ENaC plays a crucial role in regulating Na(+) absorption and extracellular fluid volume, its dysregulation causes severe phenotypes including hypertension, hypokalemia, and airway obstruction. Despite the importance of ENaC, its protein quality control mechanism remains less established. Here we firstly show the role of calreticulin (CRT), a lectin-like molecular chaperone in the endoplasmic reticulum (ER), on the regulation of ENaC...
November 15, 2009: Experimental Cell Research
Xiu-Bao Chang, April Mengos, Yue-Xian Hou, Liying Cui, Timothy J Jensen, Andrei Aleksandrov, John R Riordan, Martina Gentzsch
The epithelial chloride channel CFTR is a glycoprotein that is modified by two N-linked oligosaccharides. The most common mutant CFTR protein in patients with cystic fibrosis, DeltaF508, is misfolded and retained by ER quality control. As oligosaccharide moieties of glycoproteins are known to mediate interactions with ER lectin chaperones, we investigated the role of N-linked glycosylation in the processing of wild-type and DeltaF508 CFTR. We found that N-glycosylation and ER lectin interactions are not major determinants of trafficking of wild-type and DeltaF508 from the ER to the plasma membrane...
September 1, 2008: Journal of Cell Science
Yan Wang, Xiao Fu, Stephanie Gaiser, Michael Köttgen, Albrecht Kramer-Zucker, Gerd Walz, Tomasz Wegierski
Transient receptor potential (TRP) proteins constitute a family of cation-permeable channels that are formed by homo- or heteromeric assembly of four subunits. Despite recent progress in the identification of protein domains required for the formation of tetramers, the mechanisms governing TRP channel assembly, and biogenesis in general, remain largely elusive. In particular, little is known about the involvement of regulatory proteins in these processes. Here we report that OS-9, a ubiquitously expressed endoplasmic reticulum (ER)-associated protein, interacts with the cytosolic N-terminal tail of TRPV4...
December 14, 2007: Journal of Biological Chemistry
Weiliang Xia, Yan Shen, Haiyang Xie, Shusen Zheng
The mitochondrial calcium and downstream proline-rich tyrosine kinase-2 (PyK2) signaling pathway are critical to hepatitis B virus (HBV) replication, and the endoplasmic reticulum (ER) plays an important role in intracellular calcium regulation. To investigate the role of ER in HBV replication, the HBV genome transfected HepG2.2.15 cells were treated by cyclosporine A (CsA), cyclopiazonic acid (CPA), ryanodine and U73122, which are all specific blockers of calcium channels located in either ER or mitochondria...
November 2006: Virus Research
R G Spiro
Misfolded or incompletely assembled multisubunit glycoproteins undergo endoplasmic reticulum-associated degradation (ERAD) regulated in large measure by their N-linked polymannose oligosaccharides. In this quality control system lectin interaction with Glc(3)Man(9)GlcNAc(2) glycans after trimming with endoplasmic reticulum (ER) alpha-glucosidases and alpha-mannosidases sorts out persistently unfolded glycoproteins for N-deglycosylation and proteolytic degradation. Monoglucosylated (Glc(1)Man(9)GlcNAc(2)) glycoproteins take part in the calnexin/calreticulin glucosylation-deglucosylation cycle, while the Man(8)GlcNAc(2) isomer B product of ER mannosidase I interacts with EDEM...
May 2004: Cellular and Molecular Life Sciences: CMLS
Dermott W O'Callaghan, Burcu Hasdemir, Mark Leighton, Robert D Burgoyne
KChIPs (K+ channel interacting proteins) regulate the function of A-type Kv4 potassium channels by modifying channel properties and by increasing their cell surface expression. We have explored factors affecting the localisation of Kv4.2 and the targeting of KChIP1 and other NCS proteins by using GFP-variant fusion proteins expressed in HeLa cells. ECFP-Kv4.2 expressed alone was not retained in the ER but reached the Golgi complex. In cells co-expressing ECFP-Kv4.2 and KChIP1-EYFP, the two proteins were co-localised and were mainly present on the plasma membrane...
December 1, 2003: Journal of Cell Science
Fuli Zeng, Hong Er Tian, Zhipeng Wang, Yi An, Fengyi Gao, Lijing Zhang, Fengmin Li, Lun Shan
Considering the resemblances between Eu3+ and Ca2+ in their atomic radius and structures of the valence electron, the effects of Eu3+ on amaramthin synthesis in Amarathus caudatus seedling were studied. Eu3+ had both promoting and inhibiting effects on amaramthin synthesis. The optimum promoting concentration and half inhibiting concentration of Eu3+ to synthesis of amaranthin were 0.4 mmol/L and 2.5 mmol/L, respectively. In the dark, A23187 (ions carrier) could carry Eu3+ into cells through the Ca2+ channel...
2003: Biological Trace Element Research
M Michalak, E F Corbett, N Mesaeli, K Nakamura, M Opas
The endoplasmic reticulum (ER) plays a critical role in the synthesis and chaperoning of membrane-associated and secreted proteins. The membrane is also an important site of Ca(2+) storage and release. Calreticulin is a unique ER luminal resident protein. The protein affects many cellular functions, both in the ER lumen and outside of the ER environment. In the ER lumen, calreticulin performs two major functions: chaperoning and regulation of Ca(2+) homoeostasis. Calreticulin is a highly versatile lectin-like chaperone, and it participates during the synthesis of a variety of molecules, including ion channels, surface receptors, integrins and transporters...
December 1, 1999: Biochemical Journal
A Yamamoto, H Otsu, T Yoshimori, N Maeda, K Mikoshiba, Y Tashiro
By immunogold electron microscopy we have shown that in mouse cerebellar Purkinje cells fixed by perfusion with formaldehyde-glutaraldehyde solution, the InsP3 receptor are numerously detected on the stacks of flattened cisterns (OTSU et al, (1990) Cell Struct. Funct., 15: 163-173). In the present experiment we investigated distribution, structure and properties of the stacks by conventional electronmicroscopy, lectin cytochemistry and immunoelectron microscopy. The size and number of stacks were variable depending on their intracellular localization; short stacks with 2-4 parallel cisterns predominate in the perikaryon, long stacks with 4-15 cisterns in the proximal dendrite, and long stacks with 3-4 cisterns in the distal dendrites...
October 1991: Cell Structure and Function
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