BAIT

DNM1L

DLP1, DRP1, DVLP, DYMPLE, EMPF, HDYNIV
dynamin 1-like
Homo sapiens

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission.

Koirala S, Guo Q, Kalia R, Bui HT, Eckert DM, Frost A, Shaw JM

Mitochondrial fission is mediated by the dynamin-related GTPases Dnm1/Drp1 (yeast/mammals), which form spirals around constricted sites on mitochondria. Additional membrane-associated adaptor proteins (Fis1, Mdv1, Mff, and MiDs) are required to recruit these GTPases from the cytoplasm to the mitochondrial surface. Whether these adaptors participate in both GTPase recruitment and membrane scission is not known. Here we use a yeast strain ... [more]

Proc. Natl. Acad. Sci. U.S.A. Mar. 25, 2013; 0(0); [Pubmed: 23530241]

Throughput

  • Low Throughput

Additional Notes

  • Drp1/DNM1L polymers assembled on liposomes forms increasingly wider tubes as Mid49 mole ratio is dropped
  • MiD49 slightly increases GTP hydrolysis by Drp1/DNM1L
  • The presence of Drp1/DNM1L and MiD49 increases association of both proteins with liposomes

Curated By

  • BioGRID