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Identification of Ser465 as a novel PINK1 autophosphorylation site

Overview of attention for article published in Translational Neurodegeneration, December 2017
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Title
Identification of Ser465 as a novel PINK1 autophosphorylation site
Published in
Translational Neurodegeneration, December 2017
DOI 10.1186/s40035-017-0103-7
Pubmed ID
Authors

Ji-feng Guo, Ling-yan Yao, Qi-ying Sun, Yi-ting Cui, Yang, Qian Xu, Xin-xiang Yan, Bei-sha Tang

Abstract

PINK1 (PTEN-induced putative kinase 1) gene is the causal gene for recessive familial type 6 of Parkinson's disease (PARK6), which is an early-onset autosomal recessive inherited neurodegenerative disease. PINK1 has been reported to exert both autophosphorylation and phosphorylation activity, affecting cell damage under stress and other physiological responses. However, there has been no report on the identification of PINK1 autophosphorylation sites and their physiological functions. (1) We adopted mass spectrometry assay to identify the autophosphorylation site of PINK1, and autoradiography assay was further conducted to confirm this result. (2) Kinase activity assay was used to compare the kinase activity of both Ser465 mutant PINK1 and disease-causing mutant PINK1. (3) We use Pulse-chase analysis to measure whether Ser465 may affect PINK1 degradation. (4) Immunocytochemistry staining was used to study the PINK1 subcellular localization and Parkin transition in subcellular level. In our study, we identified the 465th serine residue (Ser465) as one of the autophosphorylation sites in PINK1 protein. The inactivation of Ser465 can decrease the kinase activity of PINK1. Either dissipated or excessive Ser465 site phosphorylation of PINK1 can slow down its degradation. PINK1 autophosphorylation contributes to the transit of Parkin to mitochondria, and has no effect on its subcellular localization. PARK6 causal mutations, T313 M and R492X, display the same characteristics as Ser465A mutation PINK1 protein, such as decreasing PINK1 kinase activity and affecting its interaction with Parkin. Ser465 was identified as one of the autophosphorylation sites of PINK1, which affected PINK1 kinase activity. In addition, Ser465 is involved in the degradation of PINK1 and the transit of Parkin to mitochondria. T313 M and R492X, two novel PARK6 mutations on Thr313 and Arg492, were similar to Ser465 mutation, including decreasing PINK1 phosphorylation activity and Parkin subcellular localization.

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Mendeley readers

The data shown below were compiled from readership statistics for 18 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 18 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 4 22%
Student > Master 3 17%
Researcher 3 17%
Student > Postgraduate 2 11%
Student > Ph. D. Student 1 6%
Other 0 0%
Unknown 5 28%
Readers by discipline Count As %
Neuroscience 7 39%
Biochemistry, Genetics and Molecular Biology 2 11%
Medicine and Dentistry 2 11%
Agricultural and Biological Sciences 1 6%
Social Sciences 1 6%
Other 0 0%
Unknown 5 28%

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 20 December 2017.
All research outputs
#9,848,769
of 12,330,736 outputs
Outputs from Translational Neurodegeneration
#108
of 124 outputs
Outputs of similar age
#247,839
of 346,710 outputs
Outputs of similar age from Translational Neurodegeneration
#11
of 13 outputs
Altmetric has tracked 12,330,736 research outputs across all sources so far. This one is in the 11th percentile – i.e., 11% of other outputs scored the same or lower than it.
So far Altmetric has tracked 124 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 26.3. This one is in the 7th percentile – i.e., 7% 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 346,710 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 17th percentile – i.e., 17% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 13 others from the same source and published within six weeks on either side of this one. This one is in the 15th percentile – i.e., 15% of its contemporaries scored the same or lower than it.