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July 1, 1987The Journal of Cell BiologyOpen Access

The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.

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Population

Intestinal microvillus 110-kD protein-calmodulin complex (110K-CM)

Design

Preclinical

Authors

KCK A ConzelmanYale UniversityMMMark S. MoosekerHeart Failure / Cardiomyopathy

Discussion

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Implication

Provides mechanistic insight into microvillar contractility; extends actin-myosin paradigm to brush border but leaves open in vivo relevance.

Structured PICO

P
Population
Intestinal microvillus 110-kD protein-calmodulin complex (110K-CM)
I
Intervention
Various ionic conditions (K+, EDTA, Ca++, Mg++), F-actin, and exogenous calmodulin
O
Outcome
ATPase enzymatic activity and actin activationsurrogate

The 110K-CM complex of the intestinal microvillus functions analogously to the mechanoenzyme myosin, exhibiting actin-activated MgATPase activity.

Cite This Study

Conzelman et al. (1987) studied this question.

synapsesocial.com/papers/6a703bfcfe4101aa97e01285https://doi.org/10.1083/jcb.105.1.313
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells.1975 · 632 citations
  2. 2Dictyostelium myosin: characterization of chymotryptic fragments and localization of the heavy-chain phosphorylation site.1981 · 53 citations
  3. 3ATPase activities and actin-binding properties of subfragments of Acanthamoeba myosin IA.1986 · 102 citations
  4. 4Acanthamoeba Myosin1973 · 517 citations
  5. 5Ca++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction in vitro.1982 · 159 citations