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Study of Endoplasmic Reticulum and Mitochondria Interactions by In Situ Proximity Ligation Assay in Fixed Cells
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Desmin Interacts Directly with Mitochondria.

Alexander A Dayal1, Natalia V Medvedeva1, Tatiana M Nekrasova1

  • 1Institute of Protein Research of Russian Academy of Sciences, Vavilova st., 34, 119334 Moscow, Russia.

International Journal of Molecular Sciences
|November 4, 2020
PubMed
Summary
This summary is machine-generated.

Desmin intermediate filaments (IFs) directly bind to mitochondria, a crucial interaction for muscle cell integrity. This binding, dependent on desmin's N-terminal domain, can be disrupted by mitochondrial proteases.

Keywords:
calpaindesminintermediate filamentsmitochondria

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Area of Science:

  • Muscle cell biology
  • Intermediate filament structure
  • Mitochondrial function

Background:

  • Desmin intermediate filaments (IFs) are essential for muscle cell structural integrity.
  • Desmin IFs connect myofibrils to cellular organelles, including mitochondria.
  • Dysfunctional desmin networks impair myofibril organization and mitochondrial health.

Purpose of the Study:

  • To investigate the direct interaction between desmin and mitochondria in vitro.
  • To determine the specific desmin domains involved in mitochondrial binding.
  • To identify mechanisms that regulate desmin-mitochondria interaction.

Main Methods:

  • Utilized recombinant human desmin and isolated rat liver mitochondria for in vitro binding assays.
  • Employed a desmin mutant (Des(Y122L)) forming unit-length filaments (ULFs) for effective separation via sucrose gradient centrifugation.
  • Investigated the role of the N-terminal domain and mitochondrial cysteine protease activity.

Main Results:

  • Demonstrated that desmin directly binds to mitochondria.
  • Established that desmin's N-terminal domain is critical for this mitochondrial interaction.
  • Showed that mitochondrial cysteine protease can cleave desmin at its N-terminus, disrupting the binding.

Conclusions:

  • Desmin directly interacts with mitochondria through its N-terminal domain.
  • Mitochondrial proteases play a role in regulating desmin-mitochondria association.
  • Understanding this interaction is key to deciphering desmin's role in muscle and mitochondrial integrity.