scholarly journals The Membrane Proteins SiaQ and SiaM Form an Essential Stoichiometric Complex in the Sialic Acid Tripartite ATP-independent Periplasmic (TRAP) Transporter SiaPQM (VC1777–1779) fromVibrio cholerae

2011 ◽  
Vol 287 (5) ◽  
pp. 3598-3608 ◽  
Author(s):  
Christopher Mulligan ◽  
Andrew P. Leech ◽  
David J. Kelly ◽  
Gavin H. Thomas
Keyword(s):  
Sialic Acid ◽  
Membrane Proteins ◽  
Stoichiometric Complex

scholarly journals Glycan-protein cross-linking mass spectrometry reveals sialic acid-mediated protein networks on cell surfaces

2021 ◽  
Author(s):  
Yixuan Xie ◽  
Siyu Chen ◽  
Qiongyu Li ◽  
Ying Sheng ◽  
Michael R Alvarez ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sialic Acid ◽  
Membrane Proteins ◽  
Cell Membranes ◽  
Sialic Acids ◽  
Cross Linking ◽  
Protein Networks ◽  
Cell Surfaces ◽  
Protein Cross Linking

A cross-linking method is developed to elucidate the glycan-mediated interactions between membrane proteins through sialic acids. The method provides previously unknown extensive glycomic interactions on cell membranes. The vast majority...

Thyrotrophin binding glycoprotein isolated from bovine thyroid

1981 ◽  
Vol 96 (3) ◽  
pp. 335-341 ◽  
Author(s):  
B. Czarnocka ◽  
A. Gardas ◽  
J. Nauman
Keyword(s):  
Sialic Acid ◽  
Membrane Proteins ◽  
Plasma Membranes ◽  
Binding Capacity ◽  
Specific Interaction ◽  
Deae Cellulose ◽  
Water Extract ◽  
Minute Amount ◽  
Bovine Thyroid ◽  
Binding Glycoprotein

Abstract. A butanol-water extraction of bovine thyroid plasma membranes was used to solubilize a thyrotrophin receptor. This method was found to solubilize approximately 12% of membrane proteins and 40% of the binding capacity of thyroid membranes for [125I]TSH. Thyrotrophin binding proteins were further purified 10 times over the butanol-water extract and 70 times over the plasma membranes by means of chromatography on DEAE-cellulose and AcA-54 Ultrogel columns. Purified fractions were found to be glycoproteins containing galactose, mannose, galactosamine, glucosamine and sialic acid. A minute amount (6.0 μg per sample) of two glycoprotein fractions obtained after chromatography on AcA-54 Ultrogel caused about 50% inhibition of [125I]-TSH binding to thyroid plasma membranes. This inhibition was due to specific interaction between thyrotrophin and isolated glycoproteins.

scholarly journals Two integral membrane proteins located in the cis-middle and trans-part of the Golgi system acquire sialylated N-linked carbohydrates and display different turnovers and sensitivity to cAMP-dependent phosphorylation.

1987 ◽  
Vol 105 (1) ◽  
pp. 215-227 ◽  
Author(s):  
L Yuan ◽  
J G Barriocanal ◽  
J S Bonifacino ◽  
I V Sandoval
Keyword(s):  
Monoclonal Antibodies ◽  
Sialic Acid ◽  
Membrane Proteins ◽  
Integral Membrane Proteins ◽  
Chemical Characteristics ◽  
Dibutyryl Cyclic Amp ◽  
Complex Type ◽  
Golgi System ◽  
Different Parts

The localization and chemical characteristics of two Golgi integral membrane proteins (GIMPs) have been studied using monoclonal antibodies. The two proteins are segregated in different parts of the Golgi system and whereas GIMPc(130 kD) is located in the cis and medial cisternae, GIMPt (100 kD) is confined in the trans-most cisterna and trans-tubular network. Both GIMPs are glycoproteins that contain N- and O-linked carbohydrates. The N-linked carbohydrates were exclusively of the complex type. Although excluded from the trans-side of the Golgi system, where sialylation is believed to occur, GIMPc acquires sialic acid in both its N- and O-linked carbohydrates. Sialic acid was also detected in the N-linked carbohydrates of GIMPt. GIMPc is apparently phosphorylated in the luminal domain in vivo. Phosphorylation occurred exclusively on serine and was stimulated by dibutyryl cyclic AMP. GIMPc and GIMPt displayed half-lives of 20 and 9 h, respectively.

scholarly journals Measurement of sialic acid content on recombinant membrane proteins

2011 ◽  
Vol 5 (S8) ◽  
Author(s):  
Deniz Baycin-Hizal ◽  
Sunny Mai ◽  
Daniel Wolozny ◽  
Ilhan Akan ◽  
Noboru Tomiya ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Membrane Proteins ◽  
Acid Content ◽  
Sialic Acid Content

scholarly journals Endoplasmic Reticulum Degradation Requires Lumen to Cytosol Signaling

2000 ◽  
Vol 151 (1) ◽  
pp. 69-82 ◽  
Author(s):  
Richard G. Gardner ◽  
Gwendolyn M. Swarbrick ◽  
Nathan W. Bays ◽  
Stephen R. Cronin ◽  
Sharon Wilhovsky ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Transmembrane Domain ◽  
Lumenal Domain ◽  
Stoichiometric Complex ◽  
Er Membrane

Endoplasmic reticulum (ER)-associated degradation (ERAD) is required for ubiquitin-mediated destruction of numerous proteins. ERAD occurs by processes on both sides of the ER membrane, including lumenal substrate scanning and cytosolic destruction by the proteasome. The ER resident membrane proteins Hrd1p and Hrd3p play central roles in ERAD. We show that these two proteins directly interact through the Hrd1p transmembrane domain, allowing Hrd1p stability by Hrd3p-dependent control of the Hrd1p RING-H2 domain activity. Rigorous reevaluation of Hrd1p topology demonstrated that the Hrd1p RING-H2 domain is located and functions in the cytosol. An engineered, completely lumenal, truncated version of Hrd3p functioned normally in both ERAD and Hrd1p stabilization, indicating that the lumenal domain of Hrd3p regulates the cytosolic Hrd1p RING-H2 domain by signaling through the Hrd1p transmembrane domain. Additionally, we identified a lumenal region of Hrd3p dispensable for regulation of Hrd1p stability, but absolutely required for normal ERAD. Our studies show that Hrd1p and Hrd3p form a stoichiometric complex with ERAD determinants in both the lumen and the cytosol. The HRD complex engages in lumen to cytosol communication required for regulation of Hrd1p stability and the coordination of ERAD events on both sides of the ER membrane.

Gangliosides as modulators of cell function

1992 ◽  
Vol 262 (6) ◽  
pp. C1341-C1355 ◽  
Author(s):  
C. B. Zeller ◽  
R. B. Marchase
Keyword(s):  
Signal Transduction ◽  
Plasma Membrane ◽  
Cell Adhesion ◽  
Sialic Acid ◽  
Membrane Proteins ◽  
Cell Function ◽  
Physiological Significance ◽  
Present Evidence ◽  
Experimental Systems ◽  
Outer Leaflet

Gangliosides, sialic acid-containing glycosphingolipids, are found in the outer leaflet of the plasma membrane of all vertebrate tissues and species. This report presents a brief introduction to the gangliosides and reviews thechemistry and topography of their biosynthesis. It also presents an overview of the present evidence supporting a physiological significance for the gangliosides in a variety of experimental systems. This includes consideration of their potential roles in development and cell adhesion. In addition, experimental examples in which gangliosides appear to influence signal transduction processes through their interactions with plasma membrane proteins are discussed.

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