Tail domains of myosin-1e regulate phosphatidylinositol signaling and F-actin polymerization at the ventral layer of podosomes
| Autor: | Mira Krendel, Zhen Feng, Yuhuan Zhou, Cheng-han Yu, Yage Zhang, Brian Sit, Fakun Cao |
|---|---|
| Přispěvatelé: | Drubin, David G. |
| Rok vydání: | 2019 |
| Předmět: |
Podosome
Plasma protein binding macromolecular substances Biology Myosins Phosphatidylinositols Polymerization 03 medical and health sciences chemistry.chemical_compound Mice Phosphatidylinositol Phosphates Protein Domains Cell Line Tumor Myosin Animals Humans Phosphatidylinositol Molecular Biology Actin Cytoskeleton 030304 developmental biology 0303 health sciences 030302 biochemistry & molecular biology Cell Membrane Cell Biology Articles Actins Cell biology Rats RAW 264.7 Cells chemistry Podosome assembly Podosomes Gelatin Signal transduction Podosome core Protein Binding Signal Transduction |
| Zdroj: | Molecular Biology of the Cell Zhang, Y, Cao, F, Zhou, Y, Feng, Z, Sit, B, Krendel, M, Yu, C & Drubin, D G (ed.) 2019, ' Tail domains of myosin-1e regulate phosphatidylinositol signaling and F-actin polymerization at the ventral layer of podosomes ', Molecular biology of the cell, vol. 30, no. 5, pp. 622-635 . https://doi.org/10.1091/mbc.E18-06-0398 |
| ISSN: | 1939-4586 |
| DOI: | 10.1091/mbc.E18-06-0398 |
| Popis: | During podosome formation, distinct phosphatidylinositol 3,4,5-trisphosphate lipid (PI(3,4,5)P3) production and F-actin polymerization take place at integrin-mediated adhesions. Membrane-associated actin regulation factors, such as myosin-1, serve as key molecules to link phosphatidylinositol signals to podosome assembly. Here, we report that long-tailed myosin-1e (Myo1e) is enriched at the ventral layer of the podosome core in a PI(3,4,5)P3-dependent manner. The combination of TH1 and TH2 (TH12) of Myo1e tail domains contains the essential motif for PI(3,4,5)P3-dependent membrane association and ventral localization at the podosome. TH12 KR2A (K772A and R782A) becomes dissociated from the plasma membrane. While F-actin polymerizations are initialized from the ventral layer of the podosome, TH12 precedes the recruitment of N-WASP and Arp2/3 in the initial phase of podosome formation. Overexpression of TH12, not TH12 KR2A, impedes PI(3,4,5)P3 signaling, restrains F-actin polymerization, and inhibits podosome formation. TH12 also suppresses gelatin degradation and migration speed of invadopodia-forming A375 melanoma cells. Thus, TH12 domain of Myo1e serves as a regulatory component to connect phosphatidylinositol signaling to F-actin polymerization at the podosome. |
| Databáze: | OpenAIRE |
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