By Kenneth R. Miller (Eds.)
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Extra resources for A Research Annual
It is likely that another core protein or the core proteins as a The Brush Border 39 whole inhibit tropomyosin’s binding to the core. This interesting issue has yet to be resolved. b. Fimbrin. Fimbrin belongs to another class of actin-binding proteins whose properties are independent of Ca++. , 1981b). , 1981c), a value similar to that of villin’s. , 1981b). , 1981b). , 1981b). , 1981b). Fimbrin, or a very closely related actin-binding protein, is widely distributed, as it has been localized by immunofluorescence to ruffled membranes, microspikes, stereocilia, and microvilli of various tissue culture cells (Bretscher and Weber, 1980a).
Biophys. Acta 17: 536-547. Pinto da Silva, P. (1972)J. Cell Biol. 53: 777-787. ,and Branton, D. (1970)J. Cell Biol. 45: 598-605. ,and Nicolson. L. (1974)Biochim. Biophys. Acta 363: 311-319. ,and Torrisi. M. R. (1982)J. Cell Biol. 93: 63-49. ,and Kan, F. W. K. (1984)J. Cell Biol. 99; 1156-1161. , and Branton, D. ) 232: 194-196. , Tomsi. M. , and Parkison, C. (1981) Science (Wash. DC) 213: 230-233. , and Rothstein, A. (1984) Biochim. Biophys. Acta 769: 381-389. Rash, J. E.. Johnson, T. J. , Hudson, C.
1984). However, in uitro studies to date raise serious questions about! , 1985). 1 in the brush border. Interestingly, peptide mapping and antibody cross-reactivity studies demonstrate that the 240-kd subunits of avian spectrin, fodrin, and TW 260/240 are highly related to one another but distinct from their mammalian 240-kd counterparts and further show that the 240-kd mammalian subunits are all distinct (Glenney and Glenney, 1983b, 1984b). Therefore, current in uirro work does not support the widely ascribed properties of TW 260/240 being a rootlet crosslinking or a rootlet-membrane-linking complex.