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XB-ART-22474
J Cell Biol 1993 Jul 01;1222:485-96.
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Structures linking microfilament bundles to the membrane at focal contacts.

Samuelsson SJ , Luther PW , Pumplin DW , Bloch RJ .


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We used quick-freeze, deep-etch, rotary replication and immunogold cytochemistry to identify a new structure at focal contacts. In Xenopus fibroblasts, elongated aggregates of particles project from the membrane to contact bundles of actin microfilaments. Before terminating, a single bundle of microfilaments interacts with several aggregates that appear intermittently over a distance of several microns. Aggregates are enriched in proteins believed to mediate actin-membrane interactions at focal contacts, including beta 1-integrin, vinculin, and talin, but they appear to contain less alpha-actinin and filamin. We also identified a second, smaller class of aggregates of membrane particles that contained beta 1-integrin but not vinculin or talin and that were not associated with actin microfilaments. Our results indicate that vinculin, talin, and beta 1-integrin are assembled into distinctive structures that mediate multiple lateral interactions between microfilaments and the membrane at focal contacts.

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Species referenced: Xenopus laevis
Genes referenced: actl6a actn1

References [+] :
Abercrombie, The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. 1971, Pubmed