Aktivni transport preko celičnih membran ATP-gnane črpalkebio.ijs.si/~krizaj/group/Predavanja...

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1 Aktivni transport preko celičnih membran ATP-gnane črpalke

Transcript of Aktivni transport preko celičnih membran ATP-gnane črpalkebio.ijs.si/~krizaj/group/Predavanja...

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Aktivni transport preko celičnih membran

ATP-gnane črpalke

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MCB - Chapter 15

The four classes of ATP-powered transport proteins

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MCB - Chapter 15

Model of mechanism of action of muscle-type Ca2+ ATPase(SERCA)

Km = 10-7 M

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MCB - Chapter 15

Schematic structural model for the α-subunit of muscle Ca2+ ATPase

Inhibited by thapsigargin

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Na+/K+ ATPase is the most important ion pumpin formation of the PM potential

Lehninger - Chapter 12

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MCB - Chapter 15

Na+/K+ ATPase and its mode of action

Inhibited by ouabain

KmNa+ = 0.6 mM

KmK+ = 0.2 mM

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MCB - Chapter 15

Acidification of the stomach lumen by P-class H+/K+ ATPase in parietal cells

pH 1pH 7

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Structural comparison of the V- and F-ATPases

Kawasaki-Nishi, S. et al. (2003) FEBS Lett. 545, 76-85

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Characteristics of V-ATPase subunits

Forgac, M. (2007) Nature Rev. MCB 8, 917-929

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Kawasaki-Nishi, S. et al. (2003) FEBS Lett. 545, 76-85

Electron micrographs of the V0 and V1V0 complexes

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Kawasaki-Nishi, S. et al. (2003) FEBS Lett. 545, 76-85

Structure and function of the V0 domain

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Forgac, M. (2007) Nature Rev. MCB 8, 917-929

Mechanism of proton transport by the V-ATPase

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Function of V-ATPases in exo/endocytosis and intracellular targeting

Forgac, M. (2007) Nature Rev. MCB 8, 917-929

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Functions of plasma membrane V-ATPases

Nishi, T. and Forgac, M. (2002) Nat. Rev. Mol. Cell Biol. 3, 94-103

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MCB - Chapter 15

V-class ATPases in toad bladder epithelial cells

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Regulation of V-ATPases

Cipriano, D.J. et al. (2008) BBA 1777, 599-604

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Lehninger - Chapter 12

Cotransport systemsdriven by gradients of Na+ and H +

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MCB - Chapter 15

Transport of the glucose (or an amino acid) from the intestinal lumen (or urine) into the blood

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ABC transporters

- Bacterial plasma membrane permeases

- Multidrug-resistance proteins (MDR1, MDR2)

- Cystic fibrosis transmembrane regulator (CFTR) protein

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MCB - Chapter 15

PM of many bacteria contain differentABC transporters - permeases

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MCB - Chapter 15

Schematic structural model of mammalianmultidrug-resistance (MDR) transport protein -- a general structural model of ABC transporters

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MCB - Chapter 15

Possible mechanisms of action of the MDR1 protein

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Cystic fibrosis transmembrane-conductance regulator (CFTR)protein is a Cl- channel

Lehninger - Chapter 12

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MCB - Chapter 15

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Recommended reading:

Lodish, H. et al. (2000): Transport across cell membranes. In: Molecular Cell Biology, 4th edition, W.H. Freeman and Company, New York.

Nelson, D.L. and Cox, M.M. (2000): Biological membranes and transport. In: Lehninger Principles of Biochemistry, 3th edition, Worth Publishers, New York.

Alberts, B. et al. (2002): Membrane transport of small molecules and the electrical properties of membranes. In: Molecular Biology of the Cell, 4th edition, Garland Science, New York.

Nishi, T. and Forgac, M. (2002): The vacuolar (H+)-ATPases – nature`s most versatile proton pumps. Nat. Rev. Mol. Cell Biol. 3, 94-103.

Kawasaki-Nishi, S., Nishi, T. and Forgac, M. (2003): Proton translocation driven by ATP hydrolysis in V-ATPases. FEBS Lett. 545, 76-85.

Forgac, M. (2007): Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology Nature Rev. MCB 8, 917-929.

Cipriano, D.J. et al. , M. (2008): Structure and regulation of the vacuolar ATPases. Biochim. Biophys. Acta 1777, 599-604.