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Joe Schober



cancer cell motility

microtubule and actin signaling

microtubule plus-end proteins



plasmid-based RNA interference

immunofluorescence-live cell correlative microscopy

MetaMorph image analysis

flow cytometry

cell microinjection



Proposed role of EB1 protein in cell motility. We hypothesize EB1 protein is part of signaling pathways that regulate actin dynamics at the cell edge.  An upstream event (signal) initiates protrusion. Pathways through EB1 on the plus-ends of microtubules (MT) regulate actin dynamics (lamellipodia and filopodia) and adhesion site remodeling. Our preliminary studies support a model where EB1 promotes lamellipodia protrusion, but suppresses filopodia and adhesion site formation.

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Key signaling molecules in lamellipodial and filopodial protrusion.  A stimulus initiates accumulation of membrane patches rich in lipid second messenger and IQGAP.  Rho family GTPases are recruited and activated.  Downstream effectors (IRSp53, mDia1, WAVE2 and PKC) link Rho GTPases to Arp2/3 complex and fascin activity.  Arp2/3 complex and fascin act proximal to lamellipodia and filopodia protrusion.  EB1, on microtubule plus-ends, localizes to areas of actin signaling.

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Hypothesized model of EB1 interaction in cell motility signaling. Our studies support a model in which EB1 balances lamellipodia with filopodia modes of protrusion through a pathway involving PKC and Rac1.





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