Interaction between band 3 and ankyrin begins in early compartments of the secretory pathway and is essential for band 3 processing

In many cell types, membrane proteins are specifically segregated to particular areas of the cell surface. It is known that this segregation is stabilized by anchorage proteins which interact with the cytoskeleton. However, the mechanism by which the interactions with anchorage proteins occur, as we...

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Published inThe Journal of biological chemistry Vol. 268; no. 26; pp. 19593 - 19597
Main Authors GOMEZ, S, MORGANS, C
Format Journal Article
LanguageEnglish
Published Bethesda, MD American Society for Biochemistry and Molecular Biology 15.09.1993
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Abstract In many cell types, membrane proteins are specifically segregated to particular areas of the cell surface. It is known that this segregation is stabilized by anchorage proteins which interact with the cytoskeleton. However, the mechanism by which the interactions with anchorage proteins occur, as well as whether they may also play a role in the process of sorting, is not known. Using differentiated murine erythroleukemic cells, we have investigated the association between band 3 (a major transmembrane anion exchanger), and ankyrin (a cytoplasmic protein that links band 3 to the cytoskeleton). Our data demonstrate that the association between band 3 and ankyrin occurs in the endoplasmic reticulum or the first Golgi compartment. These data support a model in which the band 3-ankyrin complex is inserted as a "cassette" at the plasma membrane into the cytoskeletal network. Biosynthetic studies on cotransfected 293 cells with cDNAs encoding band 3 and the band 3 binding fragment of ankyrin (AnK-90), suggest that ankyrin is not only responsible for the anchorage of band 3 to the cytoskeleton but is also involved in the exit of band 3 out of the endoplasmic reticulum.
AbstractList In many cell types, membrane proteins are specifically segregated to particular areas of the cell surface. It is known that this segregation is stabilized by anchorage proteins which interact with the cytoskeleton. However, the mechanism by which the interactions with anchorage proteins occur, as well as whether they may also play a role in the process of sorting, is not known. Using differentiated murine erythroleukemic cells, we have investigated the association between band 3 (a major transmembrane anion exchanger), and ankyrin (a cytoplasmic protein that links band 3 to the cytoskeleton). Our data demonstrate that the association between band 3 and ankyrin occurs in the endoplasmic reticulum or the first Golgi compartment. These data support a model in which the band 3-ankyrin complex is inserted as a "cassette" at the plasma membrane into the cytoskeletal network. Biosynthetic studies on cotransfected 293 cells with cDNAs encoding band 3 and the band 3 binding fragment of ankyrin (AnK-90), suggest that ankyrin is not only responsible for the anchorage of band 3 to the cytoskeleton but is also involved in the exit of band 3 out of the endoplasmic reticulum.
In many cell types, membrane proteins are specifically segregated to particular areas of the cell surface. It is known that this segregation is stabilized by anchorage proteins which interact with the cytoskeleton. However, the mechanism by which the interactions with anchorage proteins occur, as well as whether they may also play a role in the process of sorting, is not known. Using differentiated murine erythroleukemic cells, we have investigated the association between band 3 (a major transmembrane anion exchanger), and ankyrin (a cytoplasmic protein that links band 3 to the cytoskeleton). Our data demonstrate that the association between band 3 and ankyrin occurs in the endoplasmic reticulum or the first Golgi compartment. These data support a model in which the band 3-ankyrin complex is inserted as a "cassette" at the plasma membrane into the cytoskeletal network. Biosynthetic studies on cotransfected 293 cells with cDNAs encoding band 3 and the band 3 binding fragment of ankyrin (AnK-90), suggest that ankyrin is not only responsible for the anchorage of band 3 to the cytoskeleton but is also involved in the exit of band 3 out of the endoplasmic reticulum.
Author S Gomez
C Morgans
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Keywords Membrane protein
Vertebrata
Band 3 protein
Mammalia
Mouse
Rodentia
Cytoskeleton
Molecular interaction
Endoplasmic reticulum
Golgi apparatus
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Snippet In many cell types, membrane proteins are specifically segregated to particular areas of the cell surface. It is known that this segregation is stabilized by...
In many cell types, membrane proteins are specifically segregated to particular areas of the cell surface. It is known that this segregation is stabilized by...
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SubjectTerms Animals
Anion Exchange Protein 1, Erythrocyte - biosynthesis
Anion Exchange Protein 1, Erythrocyte - isolation & purification
Anion Exchange Protein 1, Erythrocyte - metabolism
Ankyrins - biosynthesis
Ankyrins - isolation & purification
Ankyrins - metabolism
Biological and medical sciences
Cell Differentiation
Cell Line
Cell structures and functions
Clone Cells
Cytoskeleton, cytoplasm. Intracellular movements
Fundamental and applied biological sciences. Psychology
Humans
Immunoblotting
Kidney
Leukemia, Erythroblastic, Acute
Methionine - metabolism
Mice
Microsomes - metabolism
Molecular and cellular biology
Plasmids
Protein Binding
Sulfur Radioisotopes
Transfection
Tumor Cells, Cultured
Title Interaction between band 3 and ankyrin begins in early compartments of the secretory pathway and is essential for band 3 processing
URI http://www.jbc.org/content/268/26/19593.abstract
https://www.ncbi.nlm.nih.gov/pubmed/8366103
https://search.proquest.com/docview/75940329
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