Flippases: still more questions than answers
Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this field and point to major tasks for future research. M...
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Published in: | Cellular and molecular life sciences : CMLS Vol. 65; no. 20; pp. 3119 - 3125 |
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Format: | Journal Article |
Language: | English |
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Basel : SP Birkhäuser Verlag Basel
01-10-2008
Birkhäuser-Verlag Springer Nature B.V |
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Abstract | Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this field and point to major tasks for future research. Most importantly, biochemical characterization of P₄-ATPases is required in order to clarify whether these transporters indeed are capable of catalyzing transmembrane phospholipid flipping. The β-subunit of P₄-ATPases shows unexpected similarities between the β- and γ-subunits of the Na⁺/K⁺-ATPase. It is likely that these proteins provide a similar solution to similar problems, and might have adopted similar structures to accomplish these tasks. No P₄-ATPases have been identified in the endoplasmic reticulum and it remains an intriguing possibility that, in this compartment, P₅A-ATPases are functional homologues of P₄-ATPases. |
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AbstractList | Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this field and point to major tasks for future research. Most importantly, biochemical characterization of P₄-ATPases is required in order to clarify whether these transporters indeed are capable of catalyzing transmembrane phospholipid flipping. The β-subunit of P₄-ATPases shows unexpected similarities between the β- and γ-subunits of the Na⁺/K⁺-ATPase. It is likely that these proteins provide a similar solution to similar problems, and might have adopted similar structures to accomplish these tasks. No P₄-ATPases have been identified in the endoplasmic reticulum and it remains an intriguing possibility that, in this compartment, P₅A-ATPases are functional homologues of P₄-ATPases. Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this field and point to major tasks for future research. Most importantly, biochemical characterization of P(4)-ATPases is required in order to clarify whether these transporters indeed are capable of catalyzing transmembrane phospholipid flipping. The beta-subunit of P(4)-ATPases shows unexpected similarities between the beta- and gamma-subunits of the Na+/K+-ATPase. It is likely that these proteins provide a similar solution to similar problems, and might have adopted similar structures to accomplish these tasks. No P(4)-ATPases have been identified in the endoplasmic reticulum and it remains an intriguing possibility that, in this compartment, P(5A)-ATPases are functional homologues of P(4)-ATPases. . Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this field and point to major tasks for future research. Most importantly, biochemical characterization of P 4 -ATPases is required in order to clarify whether these transporters indeed are capable of catalyzing transmembrane phospholipid flipping. The β-subunit of P 4 -ATPases shows unexpected similarities between the β- and γ-subunits of the Na + /K + -ATPase. It is likely that these proteins provide a similar solution to similar problems, and might have adopted similar structures to accomplish these tasks. No P 4 -ATPases have been identified in the endoplasmic reticulum and it remains an intriguing possibility that, in this compartment, P 5A -ATPases are functional homologues of P 4 -ATPases. Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this field and point to major tasks for future research. Most importantly, biochemical characterization of P4-ATPases is required in order to clarify whether these transporters indeed are capable of catalyzing transmembrane phospholipid flipping. The β-subunit of P4-ATPases shows unexpected similarities between the β- and γ-subunits of the Na+/K+-ATPase. It is likely that these proteins provide a similar solution to similar problems, and might have adopted similar structures to accomplish these tasks. No P4-ATPases have been identified in the endoplasmic reticulum and it remains an intriguing possibility that, in this compartment, P5A-ATPases are functional homologues of P4-ATPases. [PUBLICATION ABSTRACT] Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this field and point to major tasks for future research. Most importantly, biochemical characterization of P 4 -ATPases is required in order to clarify whether these transporters indeed are capable of catalyzing transmembrane phospholipid flipping. The β-subunit of P 4 -ATPases shows unexpected similarities between the β- and γ-subunits of the Na + /K + -ATPase. It is likely that these proteins provide a similar solution to similar problems, and might have adopted similar structures to accomplish these tasks. No P 4 -ATPases have been identified in the endoplasmic reticulum and it remains an intriguing possibility that, in this compartment, P 5A -ATPases are functional homologues of P 4 -ATPases. Our understandmg of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this field and point to major tasks for future research. Most importantly, biochemical characterization of P sub(4)-ATPases is required in order to clarify whether these transporters indeed are capable of catalyzing trans- membrane phospholipid flipping. The b-subunit of P sub(4)-ATPases shows unexpected similarities between the b- and g-subunits of the Na super(+)/K super(+)-ATPase. It is likely that these proteins provide a similar solution to similar problems, and might have adopted similar structures to accomplish these tasks. No P sub(4)-ATPases have been identified in the endoplasmic reticulum and it remains an intriguing possibility that, in this compartment, P sub(5A)-ATPases are functional homoloeues of P sub(4)-ATPases. |
Author | Poulsen, L. R López-Marqués, R. L Palmgren, M. G |
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Snippet | Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just... . Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just... Our understandmg of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases in these processes is just beginning... |
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SubjectTerms | Adenosine Triphosphatases - metabolism Amino Acid Sequence Animals Biochemistry Biomedical and Life Sciences Biomedicine Cell Biology Cellular biology Enzymes Eukaryotes Humans Life Sciences Lipid Bilayers - metabolism Lipids Membrane Proteins - chemistry Membrane Proteins - metabolism Membranes Molecular Sequence Data Phospholipid Transfer Proteins - chemistry Phospholipid Transfer Proteins - metabolism Phospholipids - metabolism Protein Transport Translocation Visions & Reflections (Minireview) |
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Title | Flippases: still more questions than answers |
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