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Crosstalk Between Hepatocyte Growth Factor and Integrin Signaling Pathways

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Crosstalk Between Hepatocyte Growth Factor and Integrin Signaling Pathways Journal of Biomedical Science (2006) 13: 215–223 215 DOI 10.1007/s11373-005-9061-7 Crosstalk between hepatocyte growth factor and integrin signaling pathways Po-Chao Chan, Shu-Yi Chen, Chun-Hwa Chen & Hong-Chen Chen* Department of Life Sciences and Graduate Institute of Biomedical Sciences, National Chung Hsing Univer- sity, 250 Kuo-Kuang road, Taichung, 40227, Taiwan Ó 2006 National Science Council, Taipei Key words: HGF, Met, integrin, FAK, crosstalk Summary Most types of normal cells require integrin-mediated attachment to extracellular matrix to be able to respond to growth factor stimulation for proliferation and survival. Therefore, a consensus that integrins are close collaborators with growth factors in signal transduction has gradually emerged. Some integrins and growth factor receptors appear to be normally in relatively close proximity, which can be induced to form complexes upon cell adhesion or growth factor stimulation. Moreover, since integrins and growth factor receptors share many common elements in their signaling pathways, it is clear tzhat there are many opportunities for integrin signals to modulate growth factor signals and vice versa. Increasing evidence indicates that integrins can crosstalk with receptor tyrosine kinases in a cell- and integrin-type-dependent manner through a variety of specific mechanisms. This review is intended specifically for summarizing recent progress uncovering how the hepatocyte growth factor receptor c-Met coordinates with integrins to transmit signals. Introduction growth factors [1]. Second, integrin-mediated cell adhesion and motility can be modulated by growth Cell adhesion to extracellular matrix (ECM) is a factors [4–6]. Third, many of the signaling mole- prerequisite for cell proliferation and survival [1]. cules associated with growth factor receptors, such The effects of ECM on cells are mainly mediated as Src, are also present in integrin complexes at by the integrins, a large family of cell surface focal adhesions [7]. Actually, many previous stud- receptors that bind to ECM components, organize ies suggested that integrins can crosstalk with the cytoskeleton, and activate intracellular signal- receptor tyrosine kinases in a cell- and integrin- ing pathways. Each integrin is composed of two type-dependent manner through a variety of spe- subunits: a and b. In mammals, 18 a and 8 b cific mechanisms [8, 9]. subunits associate in various combinations to form Most integrins activate focal adhesion kinase 24 integrins that can bind to distinct, although (FAK) which transduces signals to the down- partially overlapping, subsets of ECM proteins [2, stream through its interaction with several intra- 3]. Several lines of evidence indicate that pathways cellular signaling molecules, including the Src for integrin signaling and growth factor signaling family kinases, PI3K, phospholipase C-c1, Grb2, Cas are mechanistically linked. First, cell adhesion to p130 , and paxillin [10, 11]. FAK is well known ECM is required for cells to respond to certain for its pivotal role in the control of integrin- mediated cell functions, including cell migration, *To whom correspondence should be addressed. Tel: +886-4- cell cycle progression, and cell survival. However, 22854922; Fax: +886-4-22853469; E-mail: [email protected] increasing evidence has also suggested that FAK 216 may be a point of convergence of integrin and of the receptor [24, 25] and serve as docking sites growth factor signaling pathways. In addition to for the Grb2-associated binder-1 (Gab1) docking cell adhesion, a number of growth factors were protein [26, 27] and multiple Src homology 2 and shown to stimulate the tyrosine phosphorylation phosphotyrosine binding domain-containing pro- of FAK [12–14] through activation of the Src teins [28, 29]. In human cancers, the c-met gene has family kinases [14] and/or physical association of frequently been found to be amplified, mutated or FAK with the growth factor receptors [15]. The overexpressed [17, 18]. phosphorylation and activation of FAK in re- Recent studies indicated that HGF signaling sponse to growth factor stimulation facilitate its can crosstalk with integrin signaling through at association with other signaling molecules, thereby least three modes. First, the Met receptor physi- leading to amplification of downstream signals [14, cally associates with integrins at the plasma 15]. membrane where they reciprocally regulate each Hepatocyte growth factor (HGF), also known other. Second, HGF and integrin signaling path- as scatter factor, is a mesenchymally derived factor ways are converged to some intracellular signaling that elicits multiple cellular responses, including molecules, such as FAK and Src, which further proliferation, migration, and morphogenesis, on transduce signals to the downstream. Thirdly, various types of cells, [16–18]. The diverse biolog- HGF signaling leads to alteration in the expression ical effects of HGF are transmitted through of integrins that is essential for the biological activation of its transmembrane receptor encoded activities of HGF. by the c-met proto-oncogene [19]. The Met recep- tor is a heterodimer composed of a 45-kDa a chain that remains entirely extracellular, and a 145-kDa Met-integrin interplay at the plasma membrane b chain that traverses the plasma membrane and contains the intracellular tyrosine kinase domain The HGF receptor c-Met engages in reciprocal [20, 21]. Upon HGF binding, the intrinsic tyrosine regulation with integrins at the plasma membrane kinase of the receptor is activated resulting in (Figure 1). The a6b4 integrin has been shown to autophosphorylation on specific tyrosine residues cooperate with the function of HGF and its in the b chain [22, 23]. Two tyrosine residues in the receptor c-Met in carcinoma cells, resulting in COOH-terminus of the b chain (Tyr-1349 and enhanced invasive growth [30]. Upon c-Met acti- Tyr-1356) are required for all biological activities vation, a6b4 integrin physically associates with Figure 1. c-Met and integrin interplay at the plasma membrane. (a) In response to HGF stimulation, a6b4 integrin physically asso- ciates with c-Met and undergoes tyrosine phosphorylation on the b4 cytoplasmic domain, which subsequently forms a complex with Shc and PI3K, thereby potentiating Ras and PI3K signaling. The interaction of the b4 cytoplasmic domain with the adaptor protein Shc is required for HGF-induced invasion of cancer cells. (b) Ligand-independent activation of c-Met by cell adhesion. However, integrin specificity and the mechanism responsible for this form of c-Met activation remain unclear. 217 c-Met and undergoes tyrosine phosphorylation on key residue that is normally phosphorylated after the b4 cytoplasmic domain, which subsequently EGF stimulation. However, four other tyrosines forms a complex with Shc and PI3K, thereby are phosphorylated normally [39]. potentiating Ras and PI3K signaling (Figure 1a). Intracellular signaling, called ‘‘inside-out’’ sig- The a6b4 integrin is somewhat special among naling, controls the interaction between integrins other integrins in that the b4 subunit contains an and ligands [5, 6]. This cell type-specific process unusually long cytoplasmic domain, which pro- modulates integrin affinity, which is caused by a vides this integrin with additional Shc binding sites conformational change and modulation of lateral to the Met- a6b4 receptor complex, thereby diffusion and/or integrin clustering. HGF has amplifying Met signaling above a critical threshold been shown to activate integrin avb3 in epithelial for invasive behavior. The extracellular domain of cells [40], avb3 and a5b1 in endothelial cells [41], the b4 integrin is not required for its cooperation LFA-1 (aM b2) in colon cancer cells and neu- with the activated c-Met, suggesting an adhesion- trophils [42, 43], and a4b1 in B cells [44, 45]. In independent role for this integrin. In addition, the contrast, HGF was reported to inhibit aIIbb3 a6b4 integrin also associates with the epidermal activation in platelet cells [46]. Nevertheless, the growth factor (EGF) receptor family member mechanisms underlying those phenomena are ErbB2 in carcinoma cells [31]. Again, the b4 unclear. cytoplasmic domain as a monomer is necessary and sufficient to associate with ErbB2, whereas the extracellular domain, and hence matrix binding, is FAK serves as a point of convergence of HGF not required for this function [32]. and integrin signaling pathways in the cytoplasm Integrins, on the other hand, can induce various growth factor receptors to undergo Although a number of growth factors are known ligand-independent activation, at least to the to modulate cell motility, HGF is unique because extent of enhanced tyrosine phosphorylation after of the intensity with which it stimulates cell cell adhesion [33–37]. It has been shown that the motility and induces epithelial–mesenchymal tran- majority of c-Met in certain tumor cells can be sition. Since FAK is well known for its pivotal role activated by cell attachment, presumably through in regulating integrin-mediated cell motility [11], it integrins, in the complete absence of HGF [34] was reasonable to speculate that FAK is involved (Figure 1b). Overexpression of c-Met appears to in HGF signaling and plays a role in HGF- be a prerequisite for its activation by cell adhesion. stimulated cell motility. It is now known that HGF Neither the integrity of the actin cytoskeleton nor rapidly induces an increase in FAK phosphoryla- FAK activation is required for this form of c-Met tion
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