Dynamin-related Protein 1
Dynamin-related Protein 1 - Related Videos
10:12
Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
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Cited by 1 •
2024
Here, we describe some established methods to determine endoplasmic reticulum (ER) stress and unfolded protein response (UPR) activation, with particular emphasis on HIV-1 infection. This article also describes a set of protocols to investigate the effect of ER stress/UPR on HIV-1 replication and virion infectivity.
11:07
Purification of the M. magneticum Strain AMB-1 Magnetosome Associated Protein MamAΔ41
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Cited by 6 •
2010
MamA is a unique Magnetosome associated protein which was shown to be involved in magnetosome activation. Here we present the purification protocol of MamA deletion mutant (MamAΔ41) from M. magneticum AMB-1.
08:04
Overlapping Peptide Library to Map Qa-1 Epitopes in a Protein
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Cited by 4 •
2017
Qa-1 (HLA-E in human) belongs to a group of non-classical major histocompatibility complex 1b molecules. Immunization with Qa-1-binding epitopes has been shown to augment tissue-specific immune regulation and ameliorate several autoimmune diseases. Herein we describe an overlapping peptide library strategy for the identification of Qa-1 epitopes in a protein.
08:23
2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
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Cited by 10 •
2018
Protein-protein and protein-metabolite interactions are crucial for all cellular functions. Herein, we describe a protocol that allows parallel analysis of these interactions with a protein of choice. Our protocol was optimized for plant cell cultures and combines affinity purification with mass spectrometry-based protein and metabolite detection.
08:38
Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
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Cited by 27 •
2015
Proteins interact with each other and these interactions determine in a large part their functions. Protein interaction partners can be identified at high-throughput in vivo using a yeast fitness assay based on the dihydrofolate reductase protein-fragment complementation assay (DHFR-PCA).
FAQs
Fission signals prompt Dynamin-related Protein 1 to move from the cytosol to the mitochondrial outer membrane. At selected constriction sites, individual molecules assemble into spiral or ring-like oligomers. This localized recruitment is important because it concentrates the protein’s membrane-remodeling activity where a mitochondrion must be narrowed and separated.
GTP hydrolysis supplies the trigger for conformational changes within Drp1 assemblies. These changes tighten the spiral or ring-like structures surrounding a mitochondrial constriction, increasing the mechanical remodeling associated with division. The biochemical coupling between nucleotide hydrolysis and structural tightening explains how Drp1 activity can convert assembly at the membrane into scission.
Oligomerization organizes Drp1 into larger structures capable of encircling mitochondrial constriction sites. Spiral and ring-like arrangements provide a coordinated framework for tightening around the membrane rather than relying on isolated protein molecules. Their assembly therefore connects Drp1’s molecular structure with the physical remodeling required to produce separate mitochondrial organelles.
Drp1 research connects three biochemical levels: protein structure, membrane remodeling, and cellular energy regulation. Investigators can examine how a cytosolic GTPase is recruited, organized at a membrane, and coupled to conformational change during fission. This makes the protein a useful system for relating molecular mechanisms to changes in mitochondrial morphology and distribution.
By regulating mitochondrial division, Drp1 influences how mitochondria are distributed within the cell and how mitochondrial populations participate in quality control. Its activity also connects organelle morphology with cellular energy regulation and signaling. Consequently, changes in Drp1 regulation can have effects that extend beyond membrane shape to broader cellular organization and response.
Abnormal Drp1 regulation is associated with metabolic dysfunction, neurodegeneration, and other diseases. These links make Drp1 important for research that seeks to explain how disrupted mitochondrial division contributes to pathology. Because its activity is mechanistically connected to membrane scission, Drp1 is also being considered as a potential target for therapeutic investigation.