Literature DB >> 8967424

The spectrin-based membrane skeleton as a membrane protein-sorting machine.

K A Beck1, W J Nelson.   

Abstract

Normal cell function is dependent on the existence of membrane compartments that have unique populations of membrane proteins. Sorting of membrane proteins forms the basis for the biogenesis of distinct membrane compartments. There are many examples of membrane protein-sorting events in cells, but the molecular machinery involved is poorly understood. We discuss characteristics of a putative membrane protein-sorting machine and show that the spectrin-based membrane skeleton conforms to these characteristics. The spectrin-based membrane skeleton is a submembranous, spatially limited, two-dimensional lattice that binds a subset of membrane proteins. These properties allow the membrane skeleton to facilitate the formation of distinct membrane domains and thus reveal its potential as a membrane protein-sorting machine.

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Year:  1996        PMID: 8967424     DOI: 10.1152/ajpcell.1996.270.5.C1263

Source DB:  PubMed          Journal:  Am J Physiol        ISSN: 0002-9513


  26 in total

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2.  Dynamics of glycine receptor insertion in the neuronal plasma membrane.

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5.  Characteristics and regulation of glycine transport in Bergmann glia.

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8.  Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors.

Authors:  D W Allison; V I Gelfand; I Spector; A M Craig
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9.  Erythrocyte membrane vesiculation: model for the molecular mechanism of protein sorting.

Authors:  D W Knowles; L Tilley; N Mohandas; J A Chasis
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10.  Acrolein induces selective protein carbonylation in synaptosomes.

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