Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity.

Research output: Contribution to journal › Article

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Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity. / Conner, Matthew; Conner, Alex; Brown, JE; Bill, RM.

In: Biochemistry, Vol. 49, No. 5, 09.02.2010, p. 821-3.

Research output: Contribution to journal › Article

Harvard

Conner, M, Conner, A, Brown, JE & Bill, RM 2010, 'Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity.', Biochemistry, vol. 49, no. 5, pp. 821-3. https://doi.org/10.1021/bi902068b

APA

Conner, M., Conner, A., Brown, JE., & Bill, RM. (2010). Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity. Biochemistry, 49(5), 821-3. https://doi.org/10.1021/bi902068b

Vancouver

Conner M, Conner A, Brown JE, Bill RM. Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity. Biochemistry. 2010 Feb 9;49(5):821-3. https://doi.org/10.1021/bi902068b

Author

Conner, Matthew ; Conner, Alex ; Brown, JE ; Bill, RM. / Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity. In: Biochemistry. 2010 ; Vol. 49, No. 5. pp. 821-3.

Bibtex

@article{7d3c56523d3b4759840b2e8b260898c3,
title = "Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity.",
abstract = "It is well-known that the rapid flow of water into and out of cells is controlled by membrane proteins called aquaporins (AQPs). However, the mechanisms that allow cells to quickly respond to a changing osmotic environment are less well established. Using GFP-AQP fusion proteins expressed in HEK293 cells, we demonstrate the reversible manipulation of cellular trafficking of AQP1. AQP1 trafficking was mediated by the tonicity of the cell environment in a specific PKC- and microtubule-dependent manner. This suggests that the increased level of water transport following osmotic change may be due a phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization.",
author = "Matthew Conner and Alex Conner and JE Brown and RM Bill",
year = "2010",
month = feb,
day = "9",
doi = "10.1021/bi902068b",
language = "English",
volume = "49",
pages = "821--3",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "5",

}

RIS

TY - JOUR

T1 - Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity.

AU - Conner, Matthew

AU - Conner, Alex

AU - Brown, JE

AU - Bill, RM

PY - 2010/2/9

Y1 - 2010/2/9

N2 - It is well-known that the rapid flow of water into and out of cells is controlled by membrane proteins called aquaporins (AQPs). However, the mechanisms that allow cells to quickly respond to a changing osmotic environment are less well established. Using GFP-AQP fusion proteins expressed in HEK293 cells, we demonstrate the reversible manipulation of cellular trafficking of AQP1. AQP1 trafficking was mediated by the tonicity of the cell environment in a specific PKC- and microtubule-dependent manner. This suggests that the increased level of water transport following osmotic change may be due a phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization.

AB - It is well-known that the rapid flow of water into and out of cells is controlled by membrane proteins called aquaporins (AQPs). However, the mechanisms that allow cells to quickly respond to a changing osmotic environment are less well established. Using GFP-AQP fusion proteins expressed in HEK293 cells, we demonstrate the reversible manipulation of cellular trafficking of AQP1. AQP1 trafficking was mediated by the tonicity of the cell environment in a specific PKC- and microtubule-dependent manner. This suggests that the increased level of water transport following osmotic change may be due a phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization.

U2 - 10.1021/bi902068b

DO - 10.1021/bi902068b

M3 - Article

C2 - 20063900

VL - 49

SP - 821

EP - 823

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 5

ER -