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Assembled clathrin in erythrocytes.

D Bar-Zvi1, A E Levin, D Branton

  • 1Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.

The Journal of Biological Chemistry
|December 25, 1987
PubMed
Summary
This summary is machine-generated.

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Clathrin cages isolated from rat erythrocytes contain assembly proteins and kinase activities. Immunofluorescence confirmed these structures exist in intact cells, not artifacts of isolation.

Area of Science:

  • Cell Biology
  • Protein Biochemistry

Background:

  • Clathrin-coated vesicles are crucial for intracellular trafficking.
  • The protein composition and in-situ existence of clathrin cages require further elucidation.

Purpose of the Study:

  • To isolate and characterize clathrin cages from rat erythrocytes.
  • To confirm the in-situ presence of these structures within intact cells.

Main Methods:

  • Isolation of clathrin cages from rat erythrocytes.
  • Immunofluorescence microscopy to detect clathrin cages in intact cells.

Main Results:

  • Clathrin cages were successfully isolated from rat erythrocytes.
  • Immunofluorescence confirmed the presence of clathrin cages in intact erythrocytes, indicating they are not isolation artifacts.

Related Experiment Videos

  • Isolated cages were largely membrane-free but contained the clathrin assembly protein complex, 50-kDa kinase (pp50), and casein kinase II activity.

    • Conclusions:

    • Clathrin cages are pre-existing structures in rat erythrocytes.
    • These isolated cages possess enzymatic activities (pp50 and casein kinase II) relevant to clathrin-coated vesicle function.