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Hereditas(Beijing) >

2017 , Vol. 39 >Issue 4: 293 - 301

DOI: https://doi.org/10.16288/j.yczz.16-290

Review

The molecular mechanisms of plant plasma membrane intrinsic proteins trafficking and stress response

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  • 1. College of Life Science, Beijing Normal University, Beijing 100875, China
    2. Institute of Crop Science, Chinese Academy of Agricultural Sciences, Beijing 100081, China

Received date: 2016-08-23

  Revised date: 2017-01-18

  Online published: 2017-02-10

Supported by

the National Natural Science Foundation of China(31270365)

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Abstract

Plasma membrane intrinsic proteins (PIPs) are plant channel proteins located on the plasma membrane. PIPs transfer water, CO2 and small uncharged solutes through the plasma membrane. PIPs have high selectivity to substrates, suggestive of a central role in maintaining cellular water balance. The expression, activity and localization of PIPs are regulated at the transcriptional and post-translational levels, and also affected by environmental factors. Numerous studies indicate that the expression patterns and localizations of PIPs can change in response to abiotic stresses. In this review, we summarize the mechanisms of PIP trafficking, transcriptional and post-translational regulations, and abiotic stress responses. Moreover, we also discuss the current research trends and future directions on PIPs.

Key words： plasma membrane intrinsic proteins; trafficking routing; expressional regulation; activity regulation; abiotic stress

Cite this article

Xing Wang,Jilong Zhang,Xiuxiu Feng,Hongjie Li,Genfa Zhang . The molecular mechanisms of plant plasma membrane intrinsic proteins trafficking and stress response[J]. Hereditas(Beijing), 2017 , 39(4) : 293 -301 . DOI: 10.16288/j.yczz.16-290

References

[1] Preston GM, Carroll TP, Guggino WB, Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science, 1992, 256(5055): 385-387.
[2] Agre P. The aquaporin water channels. Proc Am Thorac Soc, 2006, 3(1): 5-13.
[3] Johanson U, Karlsson M, Johansson I, Gustavsson S, Sj?vall S, Fraysse L, Weig AR, Kjellbom P. The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for a new nomenclature for major intrinsic proteins in plants. Plant Physiol, 2001, 126(4): 1358-1369.
[4] Quigley F, Rosenberg JM, Shachar-Hill Y, Bohnert HJ. From genome to function: the Arabidopsis aquaporins. Genome Biol, 2001, 3: research0001.1.
[5] Wallace IS, Choi WG, Roberts DM. The structure, function and regulation of the nodulin 26-like intrinsic protein family of plant aquaglyceroporins. Biochim Biophys Acta, 2006, 1758(8): 1165-1175.
[6] Kammerloher W, Fischer U, Piechottka GP, Sch?ffner AR. Water channels in the plant plasma membrane cloned by immunoselection from a mammalian expression system. Plant J, 1994, 6(2): 187-199.
[7] Johansson I, Larsson C, Ek B, Kjellbom P. The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca 2+ and apoplastic water potential. Plant Cell, 1996, 8(7): 1181-1191.
[8] Kruse E, Uehlein N, Kaldenhoff R. The aquaporins. Genome Biol, 2006, 7: 206.
[9] Bienert GP, Cavez D, Besserer A, Berny MC, Gilis D, Rooman M, Chaumont F. A conserved cysteine residue is involved in disulfide bond formation between plant plasma membrane aquaporin monomers. Biochem J, 2012, 445(1): 101-111.
[10] daSilva LLP, Snapp EL, Denecke J, Lippincott-Schwartz J, Hawes C, Brandizzi F. Endoplasmic reticulum export sites and golgi bodies behave as single mobile secretory units in plant cells. Plant Cell, 2004, 16(7): 1753-1771.
[11] Hanton SL, Matheson LA, Chatre L, Brandizzi F. Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells. Plant J, 2009, 57(6): 963-974.
[12] Hachez C, Besserer A, Chevalier AS, Chaumont F. Insights into plant plasma membrane aquaporin trafficking. Trends Plant Sci, 2013, 18(6): 344-352.
[13] Miller EA, Beilharz TH, Malkus PN, Lee MCS, Hamamoto S, Orci L, Schekman R. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell, 2003, 114(4): 497-509.
[14] Zelazny E, Miecielica U, Borst JW, Hemminga MA, Chaumont F. An N-terminal diacidic motif is required for the trafficking of maize aquaporins ZmPIP2;4 and ZMPIP2;5 to the plasma membrane. Plant J,
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