LMTK3 inhibition affects microtubule stability

Mol Cancer. 2021 Mar 17;20(1):53. doi: 10.1186/s12943-021-01345-3.

Authors

Chiara Cilibrasi¹, Angeliki Ditsiou¹, Athanasios Papakyriakou², George Mavridis², Murat Eravci¹, Justin Stebbing³, Teresa Gagliano^{1

4}, Georgios Giamas⁵

Affiliations

¹ Department of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, JMS Building, Falmer, Brighton, BN1 9QG, UK.
² National Centre for Scientific Research "Demokritos", Institute of Biosciences and Applications, 15341, Athens, Greece.
³ Faculty of Medicine, Department of Surgery and Cancer, Imperial College, London, W12 0NN, UK.
⁴ Department of Medical Science, University of Udine, 33100, Udine, Italy.
⁵ Department of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, JMS Building, Falmer, Brighton, BN1 9QG, UK. g.giamas@sussex.ac.uk.

No abstract available

Keywords: Breast cancer; Kinase inhibitor; LMTK3; NUSAP1; Tubulin.

Publication types

Letter
Research Support, Non-U.S. Gov't

MeSH terms

Gene Expression Regulation / drug effects
Humans
Membrane Proteins / antagonists & inhibitors*
Membrane Proteins / chemistry
Membrane Proteins / genetics
Membrane Proteins / metabolism
Microtubule-Associated Proteins / genetics
Microtubule-Associated Proteins / metabolism
Microtubules / metabolism*
Models, Molecular
Protein Kinase Inhibitors / chemistry
Protein Kinase Inhibitors / pharmacology*
Protein Multimerization
Protein Serine-Threonine Kinases / antagonists & inhibitors*
Protein Serine-Threonine Kinases / chemistry
Protein Serine-Threonine Kinases / genetics
Protein Serine-Threonine Kinases / metabolism
Protein Stability / drug effects
Spindle Apparatus / drug effects
Spindle Apparatus / metabolism
Structure-Activity Relationship
Tubulin / chemistry
Tubulin / metabolism

Substances

Membrane Proteins
Microtubule-Associated Proteins
Protein Kinase Inhibitors
Tubulin
LMTK3 protein, human
Protein Serine-Threonine Kinases