PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators?

The highly conserved plant aquaporins, known as Plasma membrane Intrinsic Proteins (PIPs), are the main gateways for cell membrane water exchange. Years of research have described in detail the properties of the PIP2 subfamily. However, characterizing the PIP1 subfamily has been difficult due to the...

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Autor principal: Yaneff, A.
Otros Autores: Vitali, V., Amodeo, G.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Elsevier 2015
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-84947210653 
024 7 |2 cas  |a aquaporin, 215587-75-0; water, 7732-18-5; Aquaporins; Water 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a FEBLA 
100 1 |a Yaneff, A. 
245 1 0 |a PIP1 aquaporins: Intrinsic water channels or PIP2 aquaporin modulators? 
260 |b Elsevier  |c 2015 
270 1 0 |m Amodeo, G.; Departamento de Biodiversidad de Biología Experimental, Instituto de Biodiversidad y Biología Experimental (IBBEA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET)Argentina; email: amodeo@bg.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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504 |a Vandeleur, R.K., Sullivan, W., Athman, A., Jordans, C., Gilliham, M., Kaiser, B.N., Tyerman, S.D., Rapid shoot-to-root signalling regulates root hydraulic conductance via aquaporins (2014) Plant, Cell Environ., 37, pp. 520-538 
520 3 |a The highly conserved plant aquaporins, known as Plasma membrane Intrinsic Proteins (PIPs), are the main gateways for cell membrane water exchange. Years of research have described in detail the properties of the PIP2 subfamily. However, characterizing the PIP1 subfamily has been difficult due to the failure to localize to the plasma membrane. In addition, the discovery of the PIP1-PIP2 interaction suggested that PIP1 aquaporins could be regulated by a complex posttranslational mechanism that involves trafficking, heteromerization and fine-tuning of channel activity. This review not only considers the evidence and findings but also discusses the complexity of PIP aquaporins. To establish a new benchmark in PIP regulation, we propose to consider PIP1-PIP2 pairs as functional units for the purpose of future research into their physiological roles. © 2015 Federation of European Biochemical Societies.  |l eng 
593 |a Departamento de Biodiversidad de Biología Experimental, Instituto de Biodiversidad y Biología Experimental (IBBEA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET)Buenos Aires, Argentina 
690 1 0 |a HETEROMERIZATION 
690 1 0 |a OSMOTIC PERMEABILITY 
690 1 0 |a WATER CHANNEL 
690 1 0 |a AQUAPORIN 
690 1 0 |a PLASMA MEMBRANE INTRINSIC PROTEIN 1 
690 1 0 |a PLASMA MEMBRANE INTRINSIC PROTEIN 2 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a AQUAPORIN 
690 1 0 |a WATER 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTEIN FUNCTION 
690 1 0 |a PROTEIN INTERACTION 
690 1 0 |a PROTEIN STRUCTURE 
690 1 0 |a REGULATORY MECHANISM 
690 1 0 |a REVIEW 
690 1 0 |a STRUCTURE ANALYSIS 
690 1 0 |a WATER TRANSPORT 
690 1 0 |a ANIMAL 
690 1 0 |a GENE EXPRESSION REGULATION 
690 1 0 |a METABOLISM 
690 1 0 |a TRANSPORT AT THE CELLULAR LEVEL 
690 1 0 |a ANIMALS 
690 1 0 |a AQUAPORINS 
690 1 0 |a BIOLOGICAL TRANSPORT 
690 1 0 |a GENE EXPRESSION REGULATION 
690 1 0 |a WATER 
700 1 |a Vitali, V. 
700 1 |a Amodeo, G. 
773 0 |d Elsevier, 2015  |g v. 589  |h pp. 3508-3515  |k n. 23  |p FEBS Lett.  |x 00145793  |w (AR-BaUEN)CENRE-552  |t FEBS Letters 
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856 4 0 |u https://doi.org/10.1016/j.febslet.2015.10.018  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00145793_v589_n23_p3508_Yaneff  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v589_n23_p3508_Yaneff  |y Registro en la Biblioteca Digital 
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