DLP1Drp1

DLP1Drp1 refers to the dynamin-related protein 1 family, a conserved group of cytosolic GTPases that regulate mitochondrial and peroxisomal fission. In animals the protein is generally called Drp1, while in plants it is often called DLP1, with orthologs such as Dnm1 in yeast. The family shares a common architecture that includes an N-terminal GTPase domain, a middle/assembly region, and a C-terminal regulatory or GTPase effector domain. Functionally, Drp1/DLP1 is recruited from the cytosol to the outer mitochondrial membrane by receptor proteins and assembles into helical constriction rings. GTP hydrolysis provides the energy for membrane constriction, leading to fission; similar mechanisms operate on peroxisomes in several species.

Regulation of DLP1Drp1 activity is complex and involves multiple post-translational modifications, including phosphorylation at key residues (for example Ser616 and Ser637 in mammalian Drp1), ubiquitination, SUMOylation, and nitrosylation. These modifications influence mitochondrial recruitment, oligomerization, and the rate of fission, adapting dynamics to cellular conditions such as cell cycle stage and metabolic state. Cellular studies show that proper balance between fission and fusion is essential for mitochondrial distribution, quality control, and mitophagy.

Biological significance and disease relevance are highlighted by findings that DLP1Drp1 dysfunction can lead to abnormal mitochondrial morphology, impaired energy metabolism, and is associated with neurodegenerative and metabolic disorders in model systems. Research tools include genetic manipulation, live-cell imaging, and pharmacological inhibitors, though inhibitor studies can be context-dependent. Evolutionarily, DLP1Drp1 represents a conserved component of the mitochondrial dynamics machinery across eukaryotes.