Microfilament-membrane interactions in Xenopus myocytes.
We used quick-freeze, deep-etch, rotary-replication transmission electron microscopy to determine at molecular resolution the organization of microfilaments at the cytoplasmic surface of the sarcolemma of Xenopus myocytes. We demonstrate that actin microfilaments interact with the sarcolemma in two distinct ways. In one, which resembled focal contacts in Xenopus fibroblasts [Samuelsson et al., 1993: J. Cell Biol. 122:485-496], bundles of microfilaments approached the sarcolemma at sites containing aggregates of membrane-associated particles. Immunogold cytochemistry showed that these particle aggregates contained vinculin, talin and beta 1-integrin. In the second, which covered most of the cytoplasmic surface of the sarcolemma, individual actin microfilaments formed an extensive, lattice-like array. Particle aggregates associated with this array of actin microfilaments also labeled with antibodies to vinculin, talin and beta 1-integrin. The unique, lattice-like association of actin microfilaments with the membrane in Xenopus myocytes suggests that the organization of actin filaments over most of the sarcolemma is distinct from focal contacts, mediating widespread associations of the actin cytoskeleton with the cytoplasmic membrane face.
Samuelsson
S J
SJ
Department of Physiology, University of Maryland School of Medicine, Baltimore, USA.
Luther
P W
PW
Bloch
R J
RJ
D008841:Actin Cytoskeleton / Q000648:ultrastructure*; D000818:Animals; D019012:Integrin beta1 / Q000032:analysis; D008854:Microscopy, Electron / Q000379:methods; D018482:Muscle, Skeletal / Q000648:ultrastructure*; D016628:Replica Techniques; D012508:Sarcolemma / Q000648:ultrastructure*; D016608:Talin / Q000032:analysis; D016596:Vinculin / Q000032:analysis; D014981:Xenopus
D019012:Integrin beta1; D016608:Talin; D016596:Vinculin