↓ Skip to main content

The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane

Overview of attention for article published in Journal of Cell Science, August 2004
Altmetric Badge

Mentioned by

wikipedia
3 Wikipedia pages

Citations

dimensions_citation
88 Dimensions

Readers on

mendeley
86 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane
Published in
Journal of Cell Science, August 2004
DOI 10.1242/jcs.01280
Pubmed ID
Authors

Andrew J. Lindsay, Mary W. McCaffrey

Abstract

The Rab11 family of interacting proteins (Rab11-FIP) is a recently identified protein family composed of, to date, six members that interact with Rab11. They all share a highly homologous Rab11-binding domain (RBD) at their C-termini. However, apart from the RBD, they vary in their domain organization. Rab11-FIP3 and Rab11-FIP4 possess an ezrin-radixin-moesin (ERM) domain in their C-terminal half and EF hands in their N-terminal region. They have been termed class II Rab11-FIPs. The class I Rab11-FIPs, Rab coupling protein (RCP), Rip11 and Rab11-FIP2, each have a C2 phospholipid-binding domain near their N-termini. Although they are still membrane associated, truncation mutants of the class I Rab11-FIPs that lack their C2 domains display an altered subcellular distribution in vivo, indicating that this domain plays an important role in specifying their correct intracellular localization. To determine the phospholipids to which they bind, a protein phospholipid overlay assay was performed. Our results indicate that the class-I Rab11-FIPs bind preferentially to phosphatidylinositol-(3,4,5)-trisphosphate [PtdIns(3,4,5)P3] and the second messenger phosphatidic acid. Stimulation of PtdIns(3,4,5)P3 or phosphatidic acid synthesis results in the translocation of the Rab11-FIPs from a perinuclear location to the periphery of the cell. By contrast, the transferrin receptor does not translocate to the plasma membrane under these conditions. This translocation is dependent on the presence of the C2 domain, because class I Rab11-FIP green-fluorescent-protein fusions that lack the C2 domain cannot translocate to the plasma membrane. We propose that the C2 domains of the class I Rab11-FIPs function to target these proteins to 'docking sites' in the plasma membrane that are enriched in PtdIns(3,4,5)P3 and phosphatidic acid.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 86 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 1 1%
United States 1 1%
Unknown 84 98%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 27 31%
Researcher 20 23%
Student > Doctoral Student 8 9%
Professor 7 8%
Student > Master 6 7%
Other 13 15%
Unknown 5 6%
Readers by discipline Count As %
Agricultural and Biological Sciences 39 45%
Biochemistry, Genetics and Molecular Biology 25 29%
Neuroscience 7 8%
Medicine and Dentistry 4 5%
Environmental Science 2 2%
Other 3 3%
Unknown 6 7%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. 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 14 July 2018.
All research outputs
#8,518,156
of 25,383,344 outputs
Outputs from Journal of Cell Science
#3,598
of 9,206 outputs
Outputs of similar age
#21,856
of 66,402 outputs
Outputs of similar age from Journal of Cell Science
#39
of 75 outputs
Altmetric has tracked 25,383,344 research outputs across all sources so far. This one is in the 43rd percentile – i.e., 43% of other outputs scored the same or lower than it.
So far Altmetric has tracked 9,206 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 6.1. This one is in the 33rd percentile – i.e., 33% 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 66,402 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 11th percentile – i.e., 11% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 75 others from the same source and published within six weeks on either side of this one. This one is in the 9th percentile – i.e., 9% of its contemporaries scored the same or lower than it.