Work

Single molecule fluorescence reveals dimerization of myristoylated Src N‐terminal region on supported lipid bilayers

Year: 2016

Type: article

Abstract: The proto‐oncogene tyrosine‐protein kinase Src is a key element of signaling cascades involved in the invasive and metastasis‐forming capacity of cancer cells. While membrane tyrosine‐kinase receptors are known to dimerize, Src is classified as a non‐receptor kinase and assumed to remain always monomeric. Here we demonstrate the formation of stable dimers by the first domains of myristoylated Src previously shown to be sufficient for Src trafficking. Src dimers fused to green fluorescent protein (GFP) on supported lipid bilayers were identified using single‐molecule photobleaching experiments. Competition with a protein containing only native Src domains without GFP confirms that dimerization is a previously overlooked intrinsic property of Src. Dimerization is concomitant to membrane binding by the myristoylated forms of Src and may constitute a new regulation layer for the Src oncogene.

Source: ChemistrySelect

DOI: 10.1002/slct.201600117

Authors: Anabel‐Lise Le Roux, Bruno Castro, Erik T. Garbacik, Maria F. Garcia Parajo, Miquel Pons

Institutions: Institute for Research in Biomedicine, Barcelona Institute of Science and Technology, Universitat de Barcelona, Institute of Photonic Sciences, Institució Catalana de Recerca i Estudis Avançats

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,880

Funders: Institut de Ciències Fotòniques, European Commission, Universitat de Barcelona