Site-specific photo-crosslinking of Hsc70 with the KFERQ pentapeptide motif in a chaperone-mediated autophagy and microautophagy substrate in mammalian cells

The interaction between Hsc70 and the KFERQ-like pentapeptide motif was directly detected for the first time.

• Hsc70 is a molecular chaperone that assists in protein folding and degradation.
• It is involved in chaperone-mediated autophagy and endosomal microautophagy.
• The study used a photo-crosslinker to confirm the direct binding of Hsc70 to the KFERQ motif.
• A mutation that impairs Hsc70's ATPase activity significantly reduced the efficiency of this binding.
• The findings indicate that ATP allostery plays a role in the interaction of Hsc70 with the KFERQ-like pentapeptide.

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