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Vol. 10, Issue 10, 3197-3204, October 1999
5
1 Integrin Controls Cyclin D1 Expression by
Sustaining Mitogen-activated Protein Kinase Activity in Growth
Factor-treated Cells
Department of Pharmacology, University of Pennsylvania School of
Medicine, Philadelphia, Pennsylvania 19104-6084
Cyclin D1 expression is jointly regulated by growth factors and
cell adhesion to the extracellular matrix in many cell types. Growth
factors are thought to regulate cyclin D1 expression because they
stimulate sustained extracellular signal-regulated kinase (ERK)
activity. However, we show here that growth factors induce transient
ERK activity when added to suspended fibroblasts and sustained ERK
activity only when added to adherent fibroblasts. Cell attachment to
fibronectin or anti-
5
1 integrin is sufficient to sustain
the ERK signal and to induce cyclin D1 in growth factor-treated cells.
Moreover, when we force the sustained activation of ERK, by conditional
expression of a constitutively active MAP kinase/ERK kinase, we
overcome the adhesion requirement for expression of cyclin D1. Thus, at
least in part, fibroblasts are mitogen and anchorage dependent, because
integrin action allows for a sustained ERK signal and the
expression of cyclin D1 in growth factor-treated cells.
Present address: Department of Cell Biology and
Anatomy, University of Miami School of Medicine, Miami, FL 33101.
Corresponding author. E-mail address:
rka{at}pharm.med.upenn.edu.
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