Cytoskeletal components of the vertebrate neuromuscular junction: vinculin, alpha-actinin, and filamin
نویسندگان
چکیده
We have used immunocytochemical methods to investigate the cytoskeletal constituents of the vertebrate neuromuscular junction. Specific, affinity-purified antibodies to three cytoskeletal proteins, vinculin, alpha-actinin, and filamin, bound to neuromuscular junctions in sections of normal rat, mouse, chick, and Xenopus muscles. All three antibodies bound to the synaptic regions of denervated rat muscle fibers, indicating that the proteins recognized by these antibodies are associated with postsynaptic structures. The three proteins are present at the neuromuscular junction in muscle fibers of embryonic and neonatal animals, and therefore, may play an important role in its differentiation.
منابع مشابه
Cytoskeletal Components of the Vertebrate Junction: Vinculin, -Actinin, and Filamin Neuromuscular
We have used immunocytochemical methods to investigate the cytoskeletal constituents of the vertebrate neuromuscular junction. Specific, affinity-purified antibodies to three cytoskeletal proteins, vinculin, a-actinin, and filamin, bound to neuromuscular junctions in sections of normal rat, mouse, chick, and Xenopus muscles. All three antibodies bound to the synaptic regions of denervated rat m...
متن کاملMicrofilament-organizing centers in areas of cell contact: cytoskeletal interactions during cell attachment and locomotion
In this article we discuss three aspects of cell contact formation: (a) the molecular architecture of the cytomatrix in cell-to-substrate focal contacts, (b) the dynamic properties of membrane- and microfilament-associated proteins in the contact areas, and (c) the involvement of microtubules in the coordinated and directed formation of new substrate contacts during cell locomotion. We show tha...
متن کاملSupercontracted state of vertebrate smooth muscle cell fragments reveals myofilament lengths
Isolated cell preparations from chicken gizzard smooth muscle typically contain a mixture of cell fragments and whole cells. Both species are spontaneously permeable and may be preloaded with externally applied phalloidin and antibodies and then induced to contract with Mg ATP. Labeling with antibodies revealed that the cell fragments specifically lacked certain cytoskeletal proteins (vinculin,...
متن کاملLocalization of filamin in smooth muscle
The distribution of contractile and cytoskeletal proteins in smooth muscle has been mapped by immunocytochemical methods, with special reference to the localization of the actin-binding protein, filamin. Immunolabeling of ultrathin sections of polyvinylalcohol-embedded smooth muscle distinguished two domains in the smooth muscle cell: (a) actomyosin domains, made up of continuous longitudinal a...
متن کاملα-Actinin and Filamin Cooperatively Enhance the Stiffness of Actin Filament Networks
BACKGROUND The close subcellular proximity of different actin filament crosslinking proteins suggests that these proteins may cooperate to organize F-actin structures to drive complex cellular functions during cell adhesion, motility and division. Here we hypothesize that alpha-actinin and filamin, two major F-actin crosslinking proteins that are both present in the lamella of adherent cells, d...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Journal of Cell Biology
دوره 97 شماره
صفحات -
تاریخ انتشار 1983