Time and place: Tuesday the 10th of January at 13:00 hrs in the Auditorium in the Research Building at Montebello. Programme:
13:00 Pavel Krejci: Regulation of cell function by FGFR3 receptor tyrosine kinase
13:40: Vigdis Sørensen: The ER-protein LRRC59 regulates FGF1 nuclear import, cell morphology, and migration
At 13:00 hrs dr. Pavel Krejci from Medical Genetics Institute, Cedars-Sinai Medical Senter, Los Angeles
Regulation of cell function by FGFR3 receptor tyrosine kinase
In 1994, the field of bone biology was significantly advanced by the discovery that activating mutations in the FGFR3 receptor tyrosine kinase account for the common genetic form of dwarfism in humans, achondroplasia. Other conditions soon followed, with the list of human disorders caused by FGFR3 mutations now reaching at least 10. An array of vastly different diagnoses is caused by similar mutations in FGFR3, including syndromes affecting skeletal development (hypochondroplasia, achondroplasia, thanatophoric dysplasia), skin (epidermal nevi, seborrhaeic keratosis, acanthosis nigricans) and cancer (multiple myeloma, prostate and bladder carcinoma, seminoma). Despite many years of research, several aspects of FGFR3 function in disease remain obscure or controversial. As FGFR3-related skeletal dysplasias are caused by growth attenuation of the cartilage, chondrocytes appear to be unique in their response to FGFR3 activation. However, the reasons why FGFR3 inhibits chondrocyte growth while causing excessive cellular proliferation in cancer are not clear. Likewise, the full spectrum of molecular events by which FGFR3 mediates its signaling is just beginning to emerge. My lecture will focus the challenging journey to unravel the mechanisms of FGFR3 function in skeletal dysplasias, the extraordinary cellular manifestations of FGFR3 signaling in chondrocytes, and finally, the progress towards therapy for achondroplasia and cancer.
At 13:40 hrs: Vigdis Sørensen, Postdoc, PhD Department of Biochemistry, Institute for Cancer Research, The Norwegian Radium Hospital
The ER-protein LRRC59 regulates FGF1 nuclear import, cell morphology, and migration
LRRC59 is a membrane anchored, ER-localized protein with previously unknown function. We have identified LRRC59 as an intracellular interaction partner for Fibroblast growth factor 1 (FGF1) and we found that translocation of exogenous FGF1 into the cell nucleus requires LRRC59 as well as the classical nuclear import factors importin alpha and beta. LRRC59 is highly expressed in epithelial cells throughout the body and we are currently exploring other possible roles of this protein and we have found that it can regulate cell morphology and cell migration.
Refreshments are served in the lobby after the seminar
Centre for Cancer Biomedicine www.cancerbiomed.net