Connections with Connexins: the Molecular Basis of Direct Intercellular Signalingreview
Аннотация: Adjacent cells share ions, second messengers and small metabotes through intercellular channels which are present in gap junctions. This type of intercellular communication permits coordinated cellular activity, a critical feature for organ homeostasis during development and adult fe of multicellular organisms. Intercellular channels are structurally more complex than other ion channels, because a complete cell-to-cell channel spans two plasma membranes and results from the association of two half channels, or connexons, contributed separately by each of the two participating cells. Each connexon, in turn, is a multimeric assembly of protein subunits. The structural proteins comprising these channels, collectively called connexins, are members of a highly related multigene family consisting of at least 13 members. Since the cloning of the first connexin in 1986, considerable progress has been made in our understanding of the complex molecular switches that control the formation and permeabity of intercellular channels. Analysis of the mechanisms of channel assembly has revealed the selectivity of inter-connexin interactions and uncovered novel characteristics of the channel permeabity and gating behavior. Structure/function studies have begun to provide a molecular understanding of the significance of connexin diversity and demonstrated the unique regulation of connexins by tyrosine kinases and oncogenes. Finally, mutations in two connexin genes have been nked to human diseases. The development of more specific approaches (dominant negative mutants, knockouts, transgenes) to study the functional role of connexins in organ homeostasis is providing a new perception about the significance of connexin diversity and the regulation of intercellular communication.
Год издания: 1996
Авторы: Roberto Bruzzone, Thomas W. White, David L. Paul
Издательство: Wiley
Источник: European Journal of Biochemistry
Ключевые слова: Connexins and lens biology, Nicotinic Acetylcholine Receptors Study, Ion channel regulation and function
Другие ссылки: European Journal of Biochemistry (PDF)
European Journal of Biochemistry (HTML)
PubMed (HTML)
European Journal of Biochemistry (HTML)
PubMed (HTML)
Открытый доступ: bronze
Том: 238
Выпуск: 1
Страницы: 1–27