T‐cadherin is a glycosyl‐phosphatidylinositol (GPI) anchored cadherin molecule. We previously reported that T‐cadherin is normally expressed on the basal keratinocytes of the epidermis and is down‐regulated in cutaneous squamous cell carcinoma (SCC). We found that expression of T‐cadherin in cutaneous squamous carcinoma cells regulated level of surface β1 integrin, which functioned as extracellular matrix (ECM) receptor. Involvement of T‐cadherin in β1 integrin trafficking was studied using three different stable cell lines with cytomegalovirus (CMV)‐driven over‐expression, tetracycline (Tet)‐inducible expression and RNAi‐mediated suppressed expression of T‐cadherin. Pulse–chase analysis using a cholesterol‐depleting reagent and a tyrosine kinase inhibitor showed that β1 integrin mainly internalized via caveolae. Over‐expression of T‐cadherin suppressed the internalization of both β1 integrin and cholera toxin (CTX), a marker of caveolae‐mediated endocytosis. By Western blot analysis of tyrosine‐kinase target molecules, we demonstrated a reduced level of EGF receptor (EGFR)‐phosphorylation in T‐cadherin over‐expressing cells. In addition, studies using EGF and EGFR specific inhibitors revealed that EGFR activation stimulated β1 integrin internalization. Taking these results together, T‐cadherin may modulate cell–matrix adhesion in basal keratinocytes as well as invasive potency in SCC by regulating surface level of β1 integrin.