When a transmembrane channel isn't, or how biophysics and biochemistry (mis)communicate.
Biochim Biophys Acta Biomembr
; 1860(5): 1099-1104, 2018 May.
Article
em En
| MEDLINE
| ID: mdl-29408340
ABSTRACT
Annexins are a family of soluble proteins that bind to acidic phospholipids such as phosphatidylserine in a calcium-dependent manner. The archetypical member of the annexin family is annexin A5. For many years, its function remained unknown despite the availability of a high-resolution structure. This, combined with the observations of specific ion conductance in annexin-bound membranes, fueled speculations about the possible membrane-spanning forms of annexins that functioned as ion channels. The channel hypothesis remained controversial and did not gather sufficient evidence to become accepted. Yet, it continues to draw attention as a framework for interpreting indirect (e.g., biochemical) data. The goal of the mini-review is to examine the data on annexin-lipid interactions from the last ~30â¯years from the point of view of the controversy between the two lines of inquiry the well-characterized peripheral assembly of the annexins at membranes vs. their putative transmembrane insertion. In particular, the potential role of lipid rearrangements induced by annexin binding is highlighted.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Fenômenos Bioquímicos
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Anexinas
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Fenômenos Biofísicos
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Canais Iônicos
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Proteínas de Membrana
Limite:
Animals
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Humans
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article