Results 101 to 110 of about 9,677 (245)
Inhibition of tau aggregation by the CCT3 and CCT7 apical domains
Protein Science, Volume 34, Issue 6, June 2025.Abstract The eukaryotic chaperonin containing t‐complex polypeptide 1 (CCT/TRiC) is a molecular chaperone that assists protein folding in an ATP‐driven manner. It consists of two stacked identical rings that are each made up of eight distinct subunits. Here, we show that the apical domains of subunits CCT3 and CCT7 from humans are strong inhibitors of ...
Miki Ben‐Maimon +4 more
wiley +1 more source
Lis1 activates dynein motility by pairing it with dynactin [PDF]
, 2019 AbstractLissencephaly-1 (Lis1) is a key cofactor for dynein-mediated intracellular transport towards the minus-ends of microtubules (MTs). It remains unclear whether Lis1 serves as an inhibitor or an activator of mammalian dynein motility. Here we use single-molecule imaging and optical trapping to show that Lis1 does not directly alter the stepping ...
Elshenawy, Mohamed M. +5 more
openaire +2 more sources
βIII Spectrin Binds to the Arp1 Subunit of Dynactin [PDF]
Journal of Biological Chemistry, 2001 Cytoplasmic dynein is an intracellular motor responsible for endoplasmic reticulum-to-Golgi vesicle trafficking and retrograde axonal transport. The accessory protein dynactin has been proposed to mediate the association of dynein with vesicular cargo.
Elizabeth A. Holleran +5 more
openaire +3 more sources
eLife, 2016 Mitotic spindle orientation is used to generate cell fate diversity and drive proper tissue morphogenesis. A complex of NuMA and dynein/dynactin is required for robust spindle orientation in a number of cell types.
Lindsey Seldin +2 more
doaj +1 more source
Mass Spectrometry Reviews, Volume 44, Issue 3, Page 213-453, May/June 2025.Abstract The use of matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry for the analysis of carbohydrates and glycoconjugates is a well‐established technique and this review is the 12th update of the original article published in 1999 and brings coverage of the literature to the end of 2022.
David J. Harvey
wiley +1 more source
Dynactin Is Required for Transport Initiation from the Distal Axon [PDF]
Neuron, 2012 Dynactin is a required cofactor for the minus-end-directed microtubule motor cytoplasmic dynein. Mutations within the highly conserved CAP-Gly domain of dynactin cause neurodegenerative disease. Here, we show that the CAP-Gly domain is necessary to enrich dynactin at the distal end of primary neurons.
Erika L.F. Holzbaur, Armen J. Moughamian
openaire +3 more sources
Functionally distinct isoforms of dynactin are expressed in human neurons. [PDF]
Molecular Biology of the Cell, 1996 P150Glued is the largest subunit of dynactin, which binds to cytoplasmic dynein and activates vesicle transport along microtubules. We have isolated human cDNAs encoding p150Glued as well as a 135-kDa isoform; these isoforms are expressed in human brain by alternative mRNA splicing of the human DCTN1 gene.
Mariko Tokito +3 more
openaire +3 more sources
Transcription factor NF-kappaB is transported to the nucleus via cytoplasmic dynein/dynactin motor complex in hippocampal neurons. [PDF]
PLoS ONE, 2007 Long-term changes in synaptic plasticity require gene transcription, indicating that signals generated at the synapse must be transported to the nucleus. Synaptic activation of hippocampal neurons is known to trigger retrograde transport of transcription
Ilja Mikenberg +4 more
doaj +1 more source
Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport. [PDF]
PLoS Genetics, 2017 The microtubule-based motor dynein generates pulling forces for centrosome centration and mitotic spindle positioning in animal cells. How the essential dynein activator dynactin regulates these functions of the motor is incompletely understood. Here, we
Daniel J Barbosa +5 more
doaj +1 more source
Dynactin Phosphorylation Is Modulated in Response to Cellular Effectors
Biochemical and Biophysical Research Communications, 1997 Reversible protein phosphorylation has been implicated in the regulation of organelle transport by cytoplasmic dynein. Motor function may be modulated directly by the phosphorylation of dynein or through the phosphorylation of an accessory factor. Dynactin binds to cytoplasmic dynein and is a required activator for dynein-driven vesicular motility.
P. Farshori, Erika L.F. Holzbaur
openaire +3 more sources