Intracellular Transport: Solute Transport in Chloroplasts, Mitochondria, Peroxisomes and Vacuoles, and Between Organelles

Philippar, Katrin; Soll, Jürgen

doi:10.1002/9780470988862.ch7

Cited by 11 publications

(13 citation statements)

References 280 publications

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“…(ii) The consequence of cell compartmentalisation into extensive division of labour involves the exchange of metabolites and solutes between organelles and the cytosol. In turn, solute transporters mediating and regulating metabolic traffic are the bottleneck for proper functioning of plant cell metabolism (Philippar & Soll 2007). Again, plants are characterised by the existence of large multigene families of solute transporters, e.g.…”

Section: The Origin Of Preprotein and Metabolite Transport In Mitochomentioning

confidence: 99%

“…The transport capacity and selectivity, however, could be assigned to several outer envelope proteins (OEPs). Thus, the outer envelope of chloroplasts is equipped with low‐affinity, but specific, amino acid channels (the PRAT subfamily OEP16, see below), the substrate‐ and ATP‐gated OEP21 and the specifically expressed, but rather unspecific, porin‐like OEP24 (for overview see Philippar & Soll 2007; Duy et al. 2007).…”

Section: Metabolite Transportmentioning

confidence: 99%

“…Although primary nitrogen assimilation and, to a large extent, amino acid biosynthesis is located in plastids, apart from OEP16 in the outer envelope, so far only the DiT2 (glutamate/malate antiporter) major facilitator protein in the inner envelope membrane has been associated with amino acid transport (for overview see Linka & Weber 2005; Philippar & Soll 2007; Weber & Fischer 2007). In the plastid stroma, ammonium is directly assimilated into glutamate by the glutamine synthetase/glutamate synthase cycle.…”

Section: Metabolite Transportmentioning

confidence: 99%

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The plant PRAT proteins – preprotein and amino acid transport in mitochondria and chloroplasts*

et al. 2010

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The membrane proteins of the plant preprotein and amino acid transporter (PRAT) superfamily all share common structural elements, such as four membrane-spanning alpha-helices. Interestingly they display diverse localisation to outer and inner membranes of chloroplasts and mitochondria. Furthermore, they fulfil different functions in preprotein translocation as well as amino acid transport across these membranes. This review summarises current knowledge on precursor protein import and amino acid transport in plastids and mitochondria and provides an overview of the distinct tasks and features of members of the PRAT superfamily in the model plant Arabidopsis thaliana.

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Section: The Origin Of Preprotein and Metabolite Transport In Mitochomentioning

confidence: 99%

Section: Metabolite Transportmentioning

confidence: 99%

Section: Metabolite Transportmentioning

confidence: 99%

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The plant PRAT proteins – preprotein and amino acid transport in mitochondria and chloroplasts*

et al. 2010

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“…As their Gramnegative bacterial ancestors, all plastids are enclosed by 2 membranes, the outer and inner envelopes, which in addition to many biosynthetic capacities have to fulfill 2 distinct transport functions: (i) Because of their biosynthetic activity plastids are closely linked to the metabolic network of the plant cell. Thus, both envelope membranes mediate metabolite and solute exchange via specific channels and transporters (3,4). (ii) In the course of organelle evolution, most of the endosymbiont's genes were transferred to the host nucleus (5,6) and therefore plastids have to import the vast majority of their protein constituents as precursors in a posttranslational event from the cytosol.…”

mentioning

confidence: 99%

A search for factors influencing etioplast–chloroplast transition

Pudelski

Soll²,

Philippar³

2009

Proc. Natl. Acad. Sci. U.S.A.

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“…in protein secretion or photorespiration. Metabolic networking between compartments thus requires directed and coordinated exchange of biochemical pathway intermediates across organellar membranes (1). Chloroplasts and mitochondria are unique endosymbiotic cellular organelles, which like their prokaryotic ancestors are surrounded by two membranes.…”

mentioning

confidence: 99%

OEP40, a Regulated Glucose-permeable β-Barrel Solute Channel in the Chloroplast Outer Envelope Membrane

Harsman

Schock

Hemmis

et al. 2016

Journal of Biological Chemistry

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Chloroplasts and mitochondria are unique endosymbiotic cellular organelles surrounded by two membranes. Essential metabolic networking between these compartments and their hosting cells requires the exchange of a large number of biochemical pathway intermediates in a directed and coordinated fashion across their inner and outer envelope membranes. Here, we describe the identification and functional characterization of a highly specific, regulated solute channel in the outer envelope of chloroplasts, named OEP40. Loss of OEP40 function in Arabidopsis thaliana results in early flowering under cold temperature. The reconstituted recombinant OEP40 protein forms a high conductance ␤-barrel ion channel with subconductant states in planar lipid bilayers. The OEP40 channel is slightly cation-selective P K؉ /P Cl؊ ≈ 4:1 and rectifying (ı ᠬ/ı ᠭ Х 2) with a slope conductance of Ḡ max Х 690 picosiemens. The OEP40 channel has a restriction zone diameter of Х1.4 nm and is permeable for glucose, glucose 1-phosphate and glucose 6-phosphate, but not for maltose. Moreover, channel properties are regulated by trehalose 6-phosphate, which cannot permeate. Altogether, our results indicate that OEP40 is a "glucose-gate" in the outer envelope membrane of chloroplasts, facilitating selective metabolite exchange between chloroplasts and the surrounding cell.The plant cell is highly compartmentalized, containing at least seven different types of organelles that are involved in metabolism and cellular maintenance. In many cases, metabolic pathways and other cellular processes are not confined to one organelle but require the cooperation of several of them, e.g. in protein secretion or photorespiration. Metabolic networking between compartments thus requires directed and coordinated exchange of biochemical pathway intermediates across organellar membranes (1). Chloroplasts and mitochondria are unique endosymbiotic cellular organelles, which like their prokaryotic ancestors are surrounded by two membranes. The inner membrane of both organelles is derived from the bacterial plasma membrane. Surprisingly, also the outer membrane largely originated from and still resembles the outer membrane of the Gram-negative-like bacterial endosymbiont (2). In the inner chloroplast envelope membrane (IE), 5 numerous metabolite transporter proteins were identified and characterized to large detail with respect to their physiological impact and molecular mechanisms (3). These transporters are hydrophobic, polytopic, and mainly ␣-helical membrane proteins facilitating the exchange of metabolic precursors, intermediates, and final products between plastids and the cytoplasm. In contrast, the characteristic channels of the outer membranes in bacteria, chloroplasts as well as mitochondria, span the membrane in the form of ␤-strands that are organized to form a barrel-like pore structure (4). Proteins sharing this three-dimensional arrangement were implied in a variety of functions, including protein import (5). In addition, solute pores like the voltage-dependen...

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Intracellular Transport: Solute Transport in Chloroplasts, Mitochondria, Peroxisomes and Vacuoles, and Between Organelles

Cited by 11 publications

References 280 publications

The plant PRAT proteins – preprotein and amino acid transport in mitochondria and chloroplasts*

The plant PRAT proteins – preprotein and amino acid transport in mitochondria and chloroplasts*

A search for factors influencing etioplast–chloroplast transition

OEP40, a Regulated Glucose-permeable β-Barrel Solute Channel in the Chloroplast Outer Envelope Membrane

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