| Title |
Crystal structure of Lamellipodin implicates diverse functions in actin polymerization and Ras signaling
|
|---|---|
| Published in |
Protein & Cell, March 2013
|
| DOI | 10.1007/s13238-013-2082-5 |
| Pubmed ID | |
| Authors |
Yu-Chung Chang, Hao Zhang, Mark L Brennan, Jinhua Wu |
| Abstract |
The adapter protein Lamellipodin (Lpd) plays an important role in cell migration. In particular, Lpd mediates lamellipodia formation by regulating actin dynamics via interacting with Ena/VASP proteins. Its RA-PH tandem domain configuration suggests that like its paralog RIAM, Lpd may also mediate particular Ras GTPase signaling. We determined the crystal structures of the Lpd RA-PH domains alone and with an N-terminal coiled-coil region (cc-RA-PH). These structures reveal that apart from the anticipated coiled-coil interaction, Lpd may also oligomerize through a second intermolecular contact site. We then validated both oligomerization interfaces in solution by mutagenesis. A fluorescence-polarization study demonstrated that Lpd binds phosphoinositol with low affinity. Based on our crystallographic and biochemical data, we propose that Lpd and RIAM serve diverse functions: Lpd plays a predominant role in regulating actin polymerization, and its function in mediating Ras GTPase signaling is largely suppressed compared to RIAM. |
X Demographics
The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 1 | 100% |
Demographic breakdown
| Type | Count | As % |
|---|---|---|
| Members of the public | 1 | 100% |
Mendeley readers
The data shown below were compiled from readership statistics for 26 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 1 | 4% |
| Unknown | 25 | 96% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 7 | 27% |
| Researcher | 6 | 23% |
| Lecturer > Senior Lecturer | 2 | 8% |
| Unspecified | 2 | 8% |
| Lecturer | 1 | 4% |
| Other | 4 | 15% |
| Unknown | 4 | 15% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 8 | 31% |
| Agricultural and Biological Sciences | 7 | 27% |
| Unspecified | 2 | 8% |
| Medicine and Dentistry | 2 | 8% |
| Computer Science | 1 | 4% |
| Other | 2 | 8% |
| Unknown | 4 | 15% |
Attention Score in Context
This research output has an Altmetric Attention Score of 1. 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 07 September 2013.
All research outputs
#20,200,843
of 22,719,618 outputs
Outputs from Protein & Cell
#662
of 739 outputs
Outputs of similar age
#171,732
of 195,983 outputs
Outputs of similar age from Protein & Cell
#8
of 9 outputs
Altmetric has tracked 22,719,618 research outputs across all sources so far. This one is in the 1st percentile – i.e., 1% of other outputs scored the same or lower than it.
So far Altmetric has tracked 739 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 12.4. This one is in the 1st percentile – i.e., 1% 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 195,983 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 9 others from the same source and published within six weeks on either side of this one.