Rubicon homology domain

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Crystal structure of Human Rubicon protein bound to Rab7-GTP

Rubicon Homology Domain

The Rubicon homology domain is a conserved protein domain found in a variety of organisms. It plays a crucial role in the regulation of autophagy, a cellular process involved in the degradation and recycling of cellular components. The Rubicon homology domain is named after the protein Rubicon, which was the first protein identified to contain this domain.

Structure[edit | edit source]

The Rubicon homology domain is characterized by a specific sequence of amino acids that form a distinct structural motif. This domain is typically found in proteins that are involved in the regulation of autophagy and endosomal trafficking.

Function[edit | edit source]

The primary function of the Rubicon homology domain is to regulate the activity of proteins involved in autophagy and endosomal trafficking. It acts as a molecular scaffold that mediates protein-protein interactions and helps coordinate the various steps of these cellular processes.

Role in Autophagy[edit | edit source]

Autophagy is a highly regulated process that involves the formation of double-membrane vesicles called autophagosomes, which engulf cellular components for degradation. Proteins containing the Rubicon homology domain are known to play a role in the maturation and fusion of autophagosomes with lysosomes, where the engulfed material is degraded.

Clinical Implications[edit | edit source]

Dysregulation of autophagy has been implicated in various human diseases, including cancer, neurodegenerative disorders, and infectious diseases. Proteins containing the Rubicon homology domain are potential targets for therapeutic intervention in these conditions.

References[edit | edit source]

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Contributors: Prab R. Tumpati, MD