Please use this identifier to cite or link to this item: https://doi.org/10.1038/srep18491
Title: Kindlin-3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells
Authors: Qu, J
Ero, R
Feng, C
Ong, L.-T
Tan, H.-F
Lee, H.-S
Ismail, M.H
Bu, W.-T
Nama, S
Sampath, P 
Gao, Y.-G
Tan, S.-M
Keywords: antineoplastic antibiotic
beta3 integrin
cell surface receptor
GNB2L1 protein, human
guanine nucleotide binding protein
membrane protein
MIG2B protein, human
Myc protein
protein binding
rapamycin
recombinant protein
target of rapamycin kinase
tumor protein
animal
antagonists and inhibitors
Bagg albino mouse
biosynthesis
cell proliferation
chemistry
chronic myeloid leukemia
drug effects
genetics
HEK293 cell line
human
isolation and purification
K-562 cell line
knockout mouse
metabolism
mouse
pathology
ribosome
RNA interference
signal transduction
umbilical vein endothelial cell
Animals
Antibiotics, Antineoplastic
Cell Proliferation
GTP-Binding Proteins
HEK293 Cells
Human Umbilical Vein Endothelial Cells
Humans
Integrin beta3
K562 Cells
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Membrane Proteins
Mice
Mice, Inbred BALB C
Mice, Knockout
Neoplasm Proteins
Protein Binding
Proto-Oncogene Proteins c-myc
Receptors, Cell Surface
Recombinant Proteins
Ribosomes
RNA Interference
Signal Transduction
Sirolimus
TOR Serine-Threonine Kinases
Issue Date: 2015
Publisher: Nature Publishing Group
Citation: Qu, J, Ero, R, Feng, C, Ong, L.-T, Tan, H.-F, Lee, H.-S, Ismail, M.H, Bu, W.-T, Nama, S, Sampath, P, Gao, Y.-G, Tan, S.-M (2015). Kindlin-3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells. Scientific Reports 5 : 18491. ScholarBank@NUS Repository. https://doi.org/10.1038/srep18491
Rights: Attribution 4.0 International
Abstract: Kindlins are FERM-containing cytoplasmic proteins that regulate integrin-mediated cell-cell and cell-extracellular matrix (ECM) attachments. Kindlin-3 is expressed in hematopoietic cells, platelets, and endothelial cells. Studies have shown that kindlin-3 stabilizes cell adhesion mediated by ß1, ß2, and ß3 integrins. Apart from integrin cytoplasmic tails, kindlins are known to interact with other cytoplasmic proteins. Here we demonstrate that kindlin-3 can associate with ribosome via the receptor for activated-C kinase 1 (RACK1) scaffold protein based on immunoprecipitation, ribosome binding, and proximity ligation assays. We show that kindlin-3 regulates c-Myc protein expression in the human chronic myeloid leukemia cell line K562. Cell proliferation was reduced following siRNA reduction of kindlin-3 expression and a significant reduction in tumor mass was observed in xenograft experiments. Mechanistically, kindlin-3 is involved in integrin ?5ß1-Akt-mTOR-p70S6K signaling; however, its regulation of c-Myc protein expression could be independent of this signaling axis.
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/180401
ISSN: 2045-2322
DOI: 10.1038/srep18491
Rights: Attribution 4.0 International
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