scholarly journals Proactive for invasion: Reuse of matrix metalloproteinase for structural memory

2016 ◽  
Vol 213 (1) ◽  
pp. 11-13 ◽  
Author(s):  
Erika Gucciardo ◽  
Mohammad Mobashir ◽  
Kaisa Lehti

Migratory cells translocate membrane type-1 matrix metalloproteinase (MT1-MMP) to podosomes or invadosomes to break extracellular matrix barriers. In this issue, El Azzouzi et al. (2016. J. Cell. Biol. http://dx.doi.org/10.1083/jcb.201510043) describe an unexpected function for the MT1-MMP cytoplasmic domain in imprinting spatial memory for podosome reformation via assembly in membrane islets.

1997 ◽  
Vol 272 (4) ◽  
pp. 2446-2451 ◽  
Author(s):  
Eiko Ohuchi ◽  
Kazushi Imai ◽  
Yutaka Fujii ◽  
Hiroshi Sato ◽  
Motoharu Seiki ◽  
...  

2000 ◽  
Vol 275 (20) ◽  
pp. 15006-15013 ◽  
Author(s):  
Kaisa Lehti ◽  
Heli Valtanen ◽  
Sara Wickström ◽  
Jouko Lohi ◽  
Jorma Keski-Oja

1999 ◽  
Vol 274 (32) ◽  
pp. 22679-22685 ◽  
Author(s):  
Tara L. Haas ◽  
David Stitelman ◽  
Sandra J. Davis ◽  
Suneel S. Apte ◽  
Joseph A. Madri

2004 ◽  
Vol 279 (38) ◽  
pp. 40246
Author(s):  
Kaisa Lehti ◽  
Heli Valtanen ◽  
Sara A. Wickström ◽  
Jouko Lohi ◽  
Jorma Keski-Oja

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Maren Hülsemann ◽  
Colline Sanchez ◽  
Polina V. Verkhusha ◽  
Vera Des Marais ◽  
Serena P. H. Mao ◽  
...  

AbstractDuring breast cancer metastasis, cancer cell invasion is driven by actin-rich protrusions called invadopodia, which mediate the extracellular matrix degradation required for the success of the invasive cascade. In this study, we demonstrate that TC10, a member of a Cdc42 subfamily of p21 small GTPases, regulates the membrane type 1 matrix metalloproteinase (MT1-MMP)-driven extracellular matrix degradation at invadopodia. We show that TC10 is required for the plasma membrane surface exposure of MT1-MMP at these structures. By utilizing our Förster resonance energy transfer (FRET) biosensor, we demonstrate the p190RhoGAP-dependent regulation of spatiotemporal TC10 activity at invadopodia. We identified a pathway that regulates invadopodia-associated TC10 activity and function through the activation of p190RhoGAP and the downstream interacting effector Exo70. Our findings reveal the role of a previously unknown regulator of vesicular fusion at invadopodia, TC10 GTPase, in breast cancer invasion and metastasis.


2020 ◽  
Author(s):  
M. Hülsemann ◽  
S.K. Donnelly ◽  
P.V. Verkhusha ◽  
S.P.H. Mao ◽  
J.E. Segall ◽  
...  

AbstractDuring breast cancer metastasis, cancer cell invasion is driven by actin-rich protrusions called invadopodia, which mediate the extracellular matrix degradation required for the success of the invasive cascade. In this study, we demonstrated that TC10, a member of a Cdc42 subfamily of p21 small GTPases, regulates the membrane type 1 matrix metalloproteinase (MT1-MMP)-driven extracellular matrix degradation at invadopodia. We show that TC10 is required for the plasma membrane surface exposure of MT1-MMP at invadopodia. By utilizing our new Förster resonance energy transfer (FRET) biosensor, we demonstrated the p190RhoGAP-dependent regulation of spatiotemporal TC10 activity at invadopodia. We identified a pathway that regulates TC10 activity and function at invadopodia through the activation of p190RhoGAP and the downstream interacting effector Exo70 at the invadopodia sites. Our findings reveal the role of a previously unknown regulator of vesicular fusion at invadopodia, TC10, on the invasive potential of breast cancer cells during invasion and metastasis.


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