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A tissue-specific protein purification approach in Caenorhabditis elegans identifies novel interaction partners of DLG-1/Discs large

Overview of attention for article published in BMC Biology, August 2016
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  • Above-average Attention Score compared to outputs of the same age (52nd percentile)

Mentioned by

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7 tweeters

Citations

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34 Dimensions

Readers on

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105 Mendeley
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Title
A tissue-specific protein purification approach in Caenorhabditis elegans identifies novel interaction partners of DLG-1/Discs large
Published in
BMC Biology, August 2016
DOI 10.1186/s12915-016-0286-x
Pubmed ID
Authors

Selma Waaijers, Javier Muñoz, Christian Berends, João J. Ramalho, Soenita S. Goerdayal, Teck Y. Low, Adja D. Zoumaro-Djayoon, Michael Hoffmann, Thijs Koorman, Roderick P. Tas, Martin Harterink, Stefanie Seelk, Jana Kerver, Casper C. Hoogenraad, Olaf Bossinger, Baris Tursun, Sander van den Heuvel, Albert J. R. Heck, Mike Boxem

Abstract

Affinity purification followed by mass spectrometry (AP/MS) is a widely used approach to identify protein interactions and complexes. In multicellular organisms, the accurate identification of protein complexes by AP/MS is complicated by the potential heterogeneity of complexes in different tissues. Here, we present an in vivo biotinylation-based approach for the tissue-specific purification of protein complexes from Caenorhabditis elegans. Tissue-specific biotinylation is achieved by the expression in select tissues of the bacterial biotin ligase BirA, which biotinylates proteins tagged with the Avi peptide. We generated N- and C-terminal tags combining GFP with the Avi peptide sequence, as well as four BirA driver lines expressing BirA ubiquitously and specifically in the seam and hyp7 epidermal cells, intestine, or neurons. We validated the ability of our approach to identify bona fide protein interactions by identifying the known LGL-1 interaction partners PAR-6 and PKC-3. Purification of the Discs large protein DLG-1 identified several candidate interaction partners, including the AAA-type ATPase ATAD-3 and the uncharacterized protein MAPH-1.1. We have identified the domains that mediate the DLG-1/ATAD-3 interaction, and show that this interaction contributes to C. elegans development. MAPH-1.1 co-purified specifically with DLG-1 purified from neurons, and shared limited homology with the microtubule-associated protein MAP1A, a known neuronal interaction partner of mammalian DLG4/PSD95. A CRISPR/Cas9-engineered GFP::MAPH-1.1 fusion was broadly expressed and co-localized with microtubules. The method we present here is able to purify protein complexes from specific tissues. We uncovered a series of DLG-1 interactors, and conclude that ATAD-3 is a biologically relevant interaction partner of DLG-1. Finally, we conclude that MAPH-1.1 is a microtubule-associated protein of the MAP1 family and a candidate neuron-specific interaction partner of DLG-1.

Twitter Demographics

The data shown below were collected from the profiles of 7 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 105 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Germany 1 <1%
Unknown 104 99%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 23 22%
Student > Master 15 14%
Researcher 15 14%
Student > Bachelor 11 10%
Professor > Associate Professor 7 7%
Other 20 19%
Unknown 14 13%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 50 48%
Agricultural and Biological Sciences 27 26%
Engineering 2 2%
Business, Management and Accounting 2 2%
Neuroscience 2 2%
Other 6 6%
Unknown 16 15%

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 30 July 2021.
All research outputs
#11,068,470
of 19,233,288 outputs
Outputs from BMC Biology
#1,307
of 1,664 outputs
Outputs of similar age
#126,144
of 275,001 outputs
Outputs of similar age from BMC Biology
#1
of 1 outputs
Altmetric has tracked 19,233,288 research outputs across all sources so far. This one is in the 41st percentile – i.e., 41% of other outputs scored the same or lower than it.
So far Altmetric has tracked 1,664 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 20.1. This one is in the 19th percentile – i.e., 19% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 275,001 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 52% of its contemporaries.
We're also able to compare this research output to 1 others from the same source and published within six weeks on either side of this one. This one has scored higher than all of them