Phosphoprotein Regulates Integrin Endosomal Trafficking

Co-localization studies with TIRF microscopy

GFP, PEA-15, RFP, Clathrin light chain, U87MG cells, Epifluoresce, TIRF imaging U87MG_cells_epifluorescent_and_TIRF_teaser.jpg

Integrins are involved in cell-cell and cell-extracellular matrix adhesion. In addition, they mediate several signaling pathways, regulating e.g. cell motility. Caliva et al. discovered, with the help of a proteomics approach, that phosphoprotein PEA-15 is a binding partner for clathrin, AP-2, and integrin β1 in the endosome. This finding was confirmed by the researchers using TIRF microscopy which restricts fluorescence detection to the plasma membrane. Whereas classical epifluorescence microscopy could not reveal details, PEA-15 could be localized in defined spots together with clathrin and AP-2 with TIRF microscopy due to its higher signal to background ratio. The researchers further discovered that PEA-15 is involved in endosomal uptake of α5β1 integrin. So, they concluded that PEA-15 has a role in the regulation of cell motility.

Read the full article:

M.J. Caliva, W. Seok Yang, S. Young-Robbins, M. Zhou, H. Yoon, M.L. Matter, M.L. Grimes, T. Conrads, J.W. Ramos:

Proteomics analysis identifies PEA-15 as an endosomal phosphoprotein that regulates α5β1 integrin endocytosis

Scientific reports 11, Article number: 19830 (2021)

DOI: 10.1038/s41598-021-99348-z

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