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From physics to physiology at the membrane–motor interface

Nature Reviews Molecular Cell Biology volume 21, pages 61–62 (2020)Cite this article

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Force-generating motor proteins usually assemble on lipid membranes inside cells. We argue that it is important to consider this membrane as a dynamic entity that responds to cellular and metabolic demands in a manner that harnesses the force from motors to control pathogen degradation, cancer metastasis, lipid homeostasis and possibly other functions relevant to health and physiology.

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References

  1. Rao, M. & Mayor, S. Active organization of membrane constituents in living cells. Curr. Opin. Cell Biol. 29, 126–132 (2014).

    Article  CAS  Google Scholar 

  2. Pathak, D. & Mallik, R. Lipid–motor interactions: soap opera or symphony? Curr. Opin. Cell Biol. 44, 79–85 (2017).

    Article  CAS  Google Scholar 

  3. Klopfenstein, D. R. et al. Role of phosphatidylinositol(4,5)bisphosphate organization in membrane transport by the Unc104 kinesin motor. Cell 109, 347–358 (2002).

    Article  CAS  Google Scholar 

  4. Grover, R. et al. Transport efficiency of membrane-anchored kinesin-1 motors depends on motor density and diffusivity. Proc. Natl Acad. Sci. USA 113, E7185–E7193 (2016).

    Article  CAS  Google Scholar 

  5. Rai, A. et al. Dynein clusters into lipid microdomains on phagosomes to drive rapid transport toward lysosomes. Cell 164, 722–734 (2016).

    Article  CAS  Google Scholar 

  6. Wang, Z. et al. Binding of PLD2-generated phosphatidic acid to KIF5B promotes MT1–MMP surface trafficking and lung metastasis of mouse breast cancer cells. Dev. Cell 43, 186–197 (2017).

    Article  CAS  Google Scholar 

  7. Barak, P. et al. Quantitative optical trapping on single organelles in cell extract. Nat. Methods 10, 68–70 (2013).

    Article  CAS  Google Scholar 

  8. Rai, P. et al. Kinesin-dependent mechanism for controlling triglyceride secretion from the liver. Proc. Natl Acad. Sci. USA 114, 12958–12963 (2017).

    Article  CAS  Google Scholar 

  9. Gilham, D. Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates. Mol. Biol. Cell 16, 984–996 (2004).

    Article  Google Scholar 

  10. Kumar, M. et al. Insulin activates intracellular transport of lipid droplets to release triglycerides from the liver. J. Cell Biol. https://doi.org/10.1083/jcb.201903102 (2019).

    Article  PubMed  PubMed Central  Google Scholar 

Download references

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  1. Department of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, India

    Roop Mallik

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  1. Roop Mallik
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Correspondence to Roop Mallik.

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The authors declare no competing interests.

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Mallik, R. From physics to physiology at the membrane–motor interface. Nat Rev Mol Cell Biol 21, 61–62 (2020). https://doi.org/10.1038/s41580-019-0189-0

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