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FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes
Franziska Jarczowski1, Gunter Fischer, Frank Edlich
1Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle, Saale, Germany.
Biochemistry
|June 6, 2008
Summary
The testes-specific protein FKBP36 binds to clathrin and Hsp72. This interaction suggests a role for FKBP36 and Hsp72 in clathrin coat disassembly during male meiosis.
Area of Science:
- Reproductive biology
- Molecular cell biology
- Protein biochemistry
Background:
- The peptidyl-prolyl cis/trans isomerase FKBP36 is essential for male meiosis.
- Understanding its molecular interactions is key to elucidating its function.
Purpose of the Study:
- To investigate the molecular interactions of FKBP36.
- To determine the functional significance of these interactions in spermatogenesis.
Main Methods:
- Biochemical assays to identify binding partners of FKBP36.
- Site-directed mutagenesis to assess protein activity.
- Co-immunoprecipitation to confirm complex formation.
Main Results:
- The catalytic domain of FKBP36 binds to clathrin heavy chain (CHC).
- A specific mutation (R81L) confers prolyl isomerase activity to FKBP36.
- The TPR domain of FKBP36 specifically binds to Hsp72, a member of the Hsp70 family.
- FKBP36, clathrin, and Hsp72 form complexes associated with clathrin-coated vesicles in spermatocytes.
Conclusions:
- FKBP36 interacts with both clathrin and Hsp72.
- These interactions suggest a role for FKBP36 and Hsp72 in the disassembly of clathrin coats during male meiosis.
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