ArticleMolecular biology of the cell2005
Alanine scanning of Arp1 delineates a putative binding site for Jnm1/dynamitin and Nip100/p150Glued.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Dynactin integrity depends upon direct binding of dynamitin to Arp1.Molecular biology of the cell · 2014Article
- Arp11 affects dynein-dynactin interaction and is essential for dynein function in Aspergillus nidulans.Traffic (Copenhagen, Denmark) · 2008Article
- Dynactin function in mitotic spindle positioning.Traffic (Copenhagen, Denmark) · 2008Article
- Dynein-dynactin complex is essential for dendritic restriction of TM1-containing Drosophila Dscam.PloS one · 2008Article
- The actin multigene family of Paramecium tetraurelia.BMC genomics · 2007Article
- Arp10p is a pointed-end-associated component of yeast dynactin.Molecular biology of the cell · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Arp1p is the only actin-related protein (ARP) known to form actin-like filaments. Unlike actin, Arp1p functions with microtubules, as part of the dynein regulator, dynactin. Arp1p's dissimilar functions imply interactions with a distinct set of proteins. To distinguish surface features relating to Arp1p's core functions and to identify the footprint of protein interactions essential for dynactin function, we performed the first complete charge-cluster-to-alanine scanning mutagenesis of an ARP and compared the results with a similar study of actin. The Arp1p mutations revealed three nonoverlapping surfaces with distinct genetic properties. One of these surfaces encompassed a region unique to Arp1p that is crucial for Jnm1p (dynamitin/p50) and Nip100p (p150(Glued)) association as well as pointed-end associations. Unlike the actin mutations, none of the ARP1 alleles disrupt filament formation; however, one pointed-end allele delayed the elution of Arp1p on gel filtration, consistent with loss of additional subunits.
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Registered trials
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