Detergent interaction with band 3, a model polytopic membrane protein

Biochemistry ◽  
1993 ◽  
Vol 32 (4) ◽  
pp. 1172-1179 ◽  
Author(s):  
Joseph R. Casey ◽  
Reinhart A. F. Reithmeier
Keyword(s):  
Membrane Protein ◽  
Band 3 ◽  
Polytopic Membrane Protein

scholarly journals Glycosylation of multiple extracytosolic loops in Band 3, a model polytopic membrane protein

1996 ◽  
Vol 318 (2) ◽  
pp. 645-648 ◽  
Author(s):  
Lisa Y TAM ◽  
Carolina LANDOLT-MARTICORENA ◽  
Reinhart A. F. REITHMEIER
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Band 3 ◽  
Site Directed Mutagenesis ◽  
Acceptor Site ◽  
Oligosaccharyl Transferase ◽  
Transmembrane Segments ◽  
Free Translation ◽  
Reticulocyte Lysates ◽  
Polytopic Membrane Protein

N-glycosylated sites in polytopic membrane proteins are usually localized to single extracytosolic (EC) loops containing more than 30 residues [Landolt-Marticorena and Reithmeier (1994) Biochem. J. 302, 253–260]. This may be due to a biosynthetic restriction whereby only a single loop of nascent polypeptide is available to the oligosaccharyl transferase in the lumen of the endoplasmic reticulum. To test this hypothesis, two types of N-glycosylation mutants were constructed using Band 3, a polytopic membrane protein that contains up to 14 transmembrane segments and a single endogenous site of N-glycosylation at Asn-642 in EC loop 4. In the first set of mutants, an additional N-glycosylation acceptor site (Asn-Xaa-Ser/Thr) was constructed by site-directed mutagenesis in EC loop 3, with or without retention of the endogenous site. In the second set of mutants, EC loop 4 was duplicated and inserted into EC loop 2, again with or without retention of the endogenous site. Cell-free translation experiments using reticulocyte lysates showed that microsomes were able to N-glycosylate multiple EC loops in these Band 3 mutants. The acceptor site in EC loop 3 was poorly N-glycosylated, probably due to the suboptimal size (25 residues) of this EC loop. The localization of N-glycosylation sites to single EC loops in multi-span membrane proteins is probably due to the absence of suitably positioned acceptor sites on multiple loops.

Estimating Loop−Helix Interfaces in a Polytopic Membrane Protein by Deletion Analysis†

Biochemistry ◽  
1999 ◽  
Vol 38 (26) ◽  
pp. 8590-8597 ◽  
Author(s):  
Christopher D. Wolin ◽  
H. Ronald Kaback
Keyword(s):  
Membrane Protein ◽  
Deletion Analysis ◽  
Polytopic Membrane Protein

scholarly journals Cytosolic protein binding to band-3 protein inhibits endocytosis of isolated human erythrocyte membranes

1982 ◽  
Vol 207 (3) ◽  
pp. 595-598 ◽  
Author(s):  
K A Cordes ◽  
J M Salhany
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Band 3 Protein ◽  
High Affinity ◽  
Human Erythrocyte Membranes ◽  
Affinity Interaction ◽  
Cytoplasmic Side

Recent studies of haemoglobin binding to the cytoplasmic side of the erythrocyte membrane have shown that the predominant high-affinity interaction occurs with the major integral membrane protein known as band-3 protein and that this interaction may occur within the intact erythrocyte in a manner regulated by cell pH. We report here that haemoglobin and glyceraldehyde 3-phosphate dehydrogenase binding to band-3 protein in isolated membranes can inhibit endocytosis during vesiculation in vitro. The specificity of this effect was demonstrated by showing that myoglobin, which has an affinity for the membrane fully one to two orders of magnitude lower than that for haemoglobin, does not inhibit endocytosis.

Escherichia coliDiacylglycerol Kinase Is an α-Helical Polytopic Membrane Protein and Can Spontaneously Insert into Preformed Lipid Vesicles†

Biochemistry ◽  
1996 ◽  
Vol 35 (26) ◽  
pp. 8610-8618 ◽  
Author(s):  
Charles R. Sanders ◽  
Lech Czerski ◽  
Olga Vinogradova ◽  
Prakash Badola ◽  
David Song ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lipid Vesicles ◽  
Polytopic Membrane Protein

scholarly journals Endoplasmic reticulum transmembrane protein TMTC3 contributes to O-mannosylation of E-cadherin, cellular adherence, and embryonic gastrulation

2020 ◽  
Vol 31 (3) ◽  
pp. 167-183 ◽  
Author(s):  
Jill B. Graham ◽  
Johan C. Sunryd ◽  
Ketan Mathavan ◽  
Emma Weir ◽  
Ida Signe Bohse Larsen ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Transmembrane Protein ◽  
Homophilic Binding ◽  
Polytopic Membrane Protein ◽  
E Cadherin

Here we characterize TMTC3 as an ER, polytopic membrane protein with C-terminal luminal-facing TPRs, and an O-mannosyltransferase of E-cadherin. O-mannosylation of cadherins by TMTC3 affects cellular adherence, E-cadherin homophilic binding, and embryonic gastrulation, helping to explain the basis of a number of TMTC3-associated disease variants.

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