| Autor: |
K, Burridge, J, Feramisco, S, Blose |
| Rok vydání: |
1980 |
| Předmět: |
|
| Zdroj: |
Progress in clinical and biological research. 41 |
| ISSN: |
0361-7742 |
| Popis: |
The role of alpha-actinin in the attachment of actin to plasma membranes has been investigated. Double-label indirect immunofluorescence has been used to show that in lymphocytes alpha-actinin will concentrate beneath caps of aggregated surface Ig, confirming the recent report by Geiger and Singer [23]. Specific antibody-staining of SDS gels has indicated that alpha-actinin is a major component in isolated plasma membranes prepared from three different cell types by two different procedures. A fraction of this alpha-actinin is readily dissociated from these membranes wit relatively little parallel release of actin. The remaining alpha-actinin is more resistant to extraction but can be removed by prolonged dialysis against low ionic-strength buffers which also dissociate most of the actin. The dissociation characteristics of alpha-actinin from the plasma membrane lead us to suggest that alpha-actinin does not form a direct link between actin and the membrane, although it may promote and stabilize actin attachment by cross-linking adjacent actin filaments close to the membrane. During the course of our work with isolated plasma membranes we have tentatively identified a prominent component of these membranes as clathrin, the major protein of coated vesicles [8]. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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