Cross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis
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Abstract
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THATCH dimers really seem to be diffusing throughout the cytoplasm and the nucleus with no apparent localization to the actin patches or cables (Fig. 2b). This is consistent with our previous findings (ref. 44, 45). We attribute the residual co-localization of end4(1-856) and THATCH to incomplete cleavage by the 2A peptide. The localization of THATCH in ref. 44 and 45 is visualized at the endogenous expression level.
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solated THATCH dimers displayed a diffusive localization throughout the fission yeast cell, indicating a low affinity to F-actin, similarly to THATCH homologues (Fig. 2b)(44, 45). In contrast, overexpression of THATCH-ΔUSH dimers induced the formation of thick F-actin bundles and large puncta (Fig. 2c)(34)
Very Interesting! Did you ever notice THATCH dimers associated at cables when expressed at endogenous levels? Would this indicate something in the THATCH domain is contributing to patch localization? Do the (1-856) and THATCH fragments co-localize? If so, could the 2 fragments be re-associating (infrequently)?
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