Evidence map›Paper›PMID 31358728›Full record

ArticleExperimental & molecular medicine2019

RACK1 interaction with c-Src is essential for osteoclast function.

Jin Hee Park, Eutteum Jeong, Jingjing Lin, Ryeojin Ko, Ji Hee Kim, Sol Yi, Youngjin Choi, In-Cheol Kang, Daekee Lee, Soo Young Lee

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. RACK1 promotesiScience · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Jin Hee Park *Department of Life Science, Ewha Womans University, Seoul, 03760, Korea.
Eutteum Jeong *Department of Life Science, Ewha Womans University, Seoul, 03760, Korea.
Jingjing Lin *Department of Life Science, Ewha Womans University, Seoul, 03760, Korea.
Ryeojin KoDepartment of Life Science, Ewha Womans University, Seoul, 03760, Korea.
Ji Hee KimDepartment of Life Science, Ewha Womans University, Seoul, 03760, Korea.
Sol YiDepartment of Life Science, Ewha Womans University, Seoul, 03760, Korea.
Youngjin ChoiDepartment of Food Science & Technology, Hoseo University, Asan, 31499, Korea.
In-Cheol KangDepartment of Biological Science, College of Natural Science, BioChip Research Center, and Hoseo University, Asan, 31499, Korea.
Daekee LeeDepartment of Life Science, Ewha Womans University, Seoul, 03760, Korea.
Soo Young LeeDepartment of Life Science, Ewha Womans University, Seoul, 03760, Korea. leesy@ewha.ac.kr.
Ewha Womans University · KRHoseo University · KR

Funding

National Research Foundation of Korea (NRF) 2012R1A5A1048236National Research Foundation of Korea (NRF) 2016R1A2B3010699
6 · The paper itself

Abstract

The scaffolding protein receptor for activated C-kinase 1 (RACK1) mediates receptor activator of nuclear factor κΒ ligand (RANKL)-dependent activation of p38 MAPK in osteoclast precursors; however, the role of RACK1 in mature osteoclasts is unclear. The aim of our study was to identify the interaction between RACK1 and c-Src that is critical for osteoclast function. A RACK1 mutant protein (mutations of tyrosine 228 and 246 residues to phenylalanine; RACK1 Y228F/Y246F) did not interact with c-Src. The mutant retained its ability to differentiate into osteoclasts; however, the integrity of the RANKL-mediated cytoskeleton, bone resorption activity, and phosphorylation of c-Src was significantly decreased. Importantly, lysine 152 (K152) within the Src homology 2 (SH2) domain of c-Src is involved in RACK1 binding. The c-Src K152R mutant (mutation of lysine 152 into arginine) impaired the resorption of bone by osteoclasts. These findings not only clarify the role of the RACK1-c-Src axis as a key regulator of osteoclast function but will also help to develop new antiresorption therapies to prevent bone loss-related diseases.

Indexed as

Amino Acid SubstitutionAnimalsBone ResorptionCell DifferentiationCSK Tyrosine-Protein KinaseHEK293 CellsHumansMaleMiceMice, Inbred C57BLMutationNeoplasm ProteinsOsteoclastsp38 Mitogen-Activated Protein KinasesPhosphorylationProtein BindingCSK Tyrosine-Protein KinaseNeoplasm Proteinsp38 Mitogen-Activated Protein KinasesRACK1 protein, humanRACK1 protein, mouseRANK LigandReceptors for Activated C KinaseTNFSF11 protein, humanTnfsf11 protein, mouse

Identifiers

PMID31358728
PMCPMC6802652
OpenAlexW2965357196

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.