Where spectrin snuggles with ankyrin.

نویسنده

  • Philip S Low
چکیده

individual Plg-Rs to monocyte recruitment may change over time (enolase-1 early vs H2B later). These suggestions imply that different populations of Plg-Rs could be targeted to regulate inflammatory cell recruitment in a temporal or site-specific manner. The resurrection of enolase-1 as a Plg-R by the Wygrecka et al provides impetus for such comparative studies. Conflict-of-interest disclosure: The authors declare no competing financial interests. ■

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Current physical models for plasma membranes emphasize dynamic 10- to 300-nm compartments at thermodynamic equilibrium but subject to thermal fluctuations. However, epithelial lateral membranes contain micrometer-sized domains defined by an underlying membrane skeleton composed of spectrin and its partner ankyrin-G. We demonstrate that these spectrin/ankyrin-G domains exhibit local microtubule-...

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Ankyrin mediates the attachment of spectrin to transmembrane integral proteins in both erythroid and nonerythroid cells by binding to the beta-subunit of spectrin. Previous studies using enzymatic digestion, 2-nitro-5-thiocyanobenzoic acid cleavage, and rotary shadowing techniques have placed the spectrin-ankyrin binding site in the COOH-terminal third of beta-spectrin, but the precise site is ...

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عنوان ژورنال:
  • Blood

دوره 113 22  شماره 

صفحات  -

تاریخ انتشار 2009