scholarly journals Biosynthetic Mechanism of Polytopic Membrane Protein as Deduced by Study of Band 3 Protein

2006 ◽  
Vol 46 (1) ◽  
pp. 4-9
Author(s):  
Yoshito ABE ◽  
Naotaka HAMASAKI
Keyword(s):  
Membrane Protein ◽  
Band 3 ◽  
Band 3 Protein ◽  
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.

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.

scholarly journals Immunolocalization of band 3 protein in normal and cystic fibrosis skin.

1986 ◽  
Vol 34 (6) ◽  
pp. 823-826 ◽  
Author(s):  
D J Hazen-Martin ◽  
G Pasternack ◽  
S S Spicer ◽  
D A Sens
Keyword(s):  
Cystic Fibrosis ◽  
Membrane Protein ◽  
Chloride Transport ◽  
Duct Cell ◽  
Band 3 ◽  
Current Evidence ◽  
Band 3 Protein ◽  
Sweat Duct ◽  
Protein Immunoreactivity ◽  
Secretory Coil

Current evidence indicates that the defect in cystic fibrosis (CF) involves chloride transport in various epithelial cells. The sweat gland, one site of altered chloride transport in CF, was examined immunocytochemically for localization of a chloride-channel membrane protein, designated band 3 protein. Immunoreactivity was observed in sweat duct cell membranes of both normal and CF samples, whereas secretory coil regions were entirely unreactive. No difference was observed in the pattern or intensity of immunoreactivity between the two groups at the light microscopic (LM) level of resolution.

A new concept in polytopic membrane proteins following from the study of band 3 protein

1998 ◽  
Vol 76 (5) ◽  
pp. 729-733 ◽  
Author(s):  
Naotaka Hamasaki ◽  
Hiroyuki Kuma ◽  
Kazuhisa Ota ◽  
Masao Sakaguchi ◽  
Katsuyoshi Mihara
Keyword(s):  
Membrane Proteins ◽  
Transmembrane Domain ◽  
Band 3 ◽  
Band 3 Protein ◽  
Transmembrane Peptides ◽  
Lipid Interactions ◽  
Transmembrane Segments ◽  
Novel Concept ◽  
Polytopic Membrane Protein ◽  
Peptide Classification

In the present communication, we introduce a novel concept in multispanning polytopic membrane proteins revealed by the study of the band 3 protein. The transmembrane domain of such proteins can be divided into three categories, that is, hydrophilic loops connecting transmembrane peptides (category 1), portions embedded by peptide-peptide interactions (category 2), and portions embedded by peptide-lipid interactions (category 3). Category 2 peptides of polytopic membrane proteins were found to stably reside in the lipid bilayer without peptide-lipid interactions that had been thought to be essential for transmembrane segments. Category 3 peptides are equivalent to single-spanning segments of bitopic membrane proteins. Three different experiments, namely proteolytic digestion, chemical modification of the band 3 protein, and cell free transcription and translation, were used to categorize the transmembrane peptides.Key words: band 3 protein, transmembrane (TM) peptide, classification of TM, category 2-TM, polytopic membrane protein.

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
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