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Updated: Apr 27, 2026

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation
Published on: February 2, 2024
Regulation of integrin activity by phosphorylation
Carl G Gahmberg1, Mikaela Grönholm, Liisa M Uotila
1Division of Biochemistry and Biotechnology, Department of Biosciences, University of Helsinki, Viikinkaari 5, 00014, Helsinki, Finland, carl.gahmberg@helsinki.fi.
Abstract:
Integrins are heterodimeric complex type I membrane proteins involved in cellular adhesion and signaling. They exist as inactive molecules in resting cells, and need activation to become adhesive. Although much is known about their structure, and a large number of interacting molecules have been described, we still only partially understand how their activities are regulated. In this review we focus on the leukocyte-specific β2-integrins and, specifically, on the role of integrin phosphorylation in the regulation of activity. Phosphorylation reactions can be fast and reversible, thus enabling strictly directed regulatory activities both time-wise and locally in specific regions of the plasma membrane in different leukocytes.
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