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Professor Josephine C AdamsMA(Cantab.), PhD(Lond.)

Professor of Cell Biology

Jo Adams

Professor Josephine C AdamsMA(Cantab.), PhD(Lond.)

Professor of Cell Biology

Member of

Research interests

The central interest of the laboratory is in cell-matrix adhesion processes and their roles in regulating intracellular signaling and cell protrusions. We study molecular mechanisms of these processes in health and disease. Research areas focus on extracellular processes that modulate extracellular matrix organization, also on intracellular signaling pathways that regulate actin cytoskeletal organisation in cell protrusions and adhesion complexes. More details of each area are given on the laboratory Group Page.

  • Fascin-based protrusions and their role in carcinoma cell migration and metastasis: Current projects study signaling mechanisms that regulate actin-bundling by fascin in carcinoma cell migration and metastasis, examine how fascin and other components of protrusions are integrated, and assess the suitability of fascin-1 as a potential novel therapeutic target.
  • Thrombospondins and their roles in Extracellular Matrix: We are examining the evolution of thrombospondins and their conserved roles within the extracellular matrix, in particular the molecular mechanisms by which thrombospondins become deposited into the extracellular matrix through interactions with cell surfaces and other matrix components.
  • The Muskelin/RanBP9/CTLH complex: Muskelin and RanBP9 are co-associated proteins whose knockdown phenotypes in mammalian cells demonstrate functional roles in cell morphology regulation. RanBP9 mediates association with a widely-expressed protein complex, referred to as muskelin/RanBP9/CTLH complex. A homologous complex in budding yeast functions in proteosomal and vacuolar degradation of specific target proteins, however, fundamental aspects of the organisation, regulation and roles of muskelin/RanBP9/CTLH complex in mammalian cells remain unknown. We are examining the hypothesis that mammalian muskelin/RanBP9/CTLH complex regulates degradation of specific target proteins that include cytoskeletal and adhesion proteins.

More details of each area are given on the laboratory Group Page.

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Postal address:
Biomedical Sciences Building
University Walk
Clifton
Bristol
United Kingdom