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Related Experiment Videos

Organization of clathrin coat structures.

K Prasad1, R E Lippoldt

  • 1Clinical Endocrinology Branch, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892.

Biochemistry
|April 18, 1989
PubMed
Summary

Associated proteins (APs) influence clathrin polymerization, directing the formation of distinct basket sizes (150S, 220S, 300S) under specific pH conditions. Smaller baskets serve as intermediates for larger structures.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Structural Biology

Background:

  • Clathrin (8S) self-polymerizes into heterogeneous baskets (150-400S) at low pH.
  • Associated proteins (APs) from coated vesicles typically induce homogeneous clathrin polymerization.

Purpose of the Study:

  • To investigate the effect of associated proteins (APs) on clathrin polymerization dynamics.
  • To characterize the distinct basket sizes formed by clathrin in the presence of APs.

Main Methods:

  • Purification of clathrin.
  • In vitro polymerization assays at low pH (0.1 M MES, pH 6.0).
  • Analysis of polymerized clathrin structures using sedimentation coefficients and SDS-PAGE.

Main Results:

  • APs induce polymerization of clathrin into three distinct basket sizes: 150S, 220S, and 300S.
  • Clathrin to AP ratio influences basket size: lower ratios yield smaller baskets, higher ratios yield larger baskets.
  • 150S baskets are identified as intermediates in the polymerization to larger 300S baskets.

Conclusions:

  • Associated proteins (APs) play a crucial role in regulating clathrin basket size and structure.
  • Clathrin polymerization is a size-controlled process influenced by protein stoichiometry.
  • The formation of distinct clathrin basket sizes has implications for intracellular vesicle trafficking.

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