Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

PMP1 - Pmp1p

Saccharomyces cerevisiae S288c

Synonyms: Plasma membrane ATPase proteolipid 1, YCR024C-A, YCR24C-A

Beswick, V. et al., Mousson, F. et al., Navarre, C. et al., Navarre, C. et al., Hirayama, S. et al., et al.

Roux, Beswick, Coïc, Huynh-Dinh, Sanson, Neumann,

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PMP1

Interestingly, overexpression of Prz1 did not suppress the Cl(-) hypersensitivity of calcineurin deletion, and overexpression of Pmp1 MAPK phosphatase suppressed the Cl(-) hypersensitivity of calcineurin deletion but not the Ca(2+) hypersensitivity of prz1 deletion [1].

High impact information on PMP1

The two proteolipids differ at residue 21, which is an alanine in PMP1 and a serine in PMP2 [2].
A small proteolipid called PMP1 is associated with yeast plasma membrane H(+)-ATPase (Navarre, C., Ghislain, M., Leterme, S., Ferroud, C., Dufour, J.-P., and Goffeau, A. (1992) J. Biol. Chem. 267, 6425-6428) [2].
The polypeptide lacks the first two NH2-terminal amino acids as compared with the deduced sequence of the PMP1 gene (for plasma membrane proteolipid) isolated by hybridization with an oligonucleotide probe corresponding to an internal amino acid sequence of the proteolipid [3].
Mutational analysis and (1)H NMR experiments were therefore performed on a synthetic PMP1 fragment using DPC-d(38) micelles as a membrane-like environment, in the presence of small amounts of POPS [4].
Protonated DPC, DMPC and DMPS were incorporated in deuterated micelles containing the PMP1 fragment for studying lipid-peptide interactions [5].

Associations of PMP1 with chemical compounds

PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from bilayer mixtures with phosphatidylcholine: a (2)H-NMR study [6].

Analytical, diagnostic and therapeutic context of PMP1

From POPS titration experiments monitored by a full set of one- and two-dimensional NOESY spectra, the association between the phospholipids and the PMP1 peptide has been followed [4].
To investigate the molecular basis of the PMP1 biological function, the conformational properties of a synthetic PMP1 fragment, A18-F38, comprising the predicted C-terminal cytoplasmic domain and a part of the transmembrane anchor have been studied by 1H- and 2H-NMR spectroscopies [5].
Time-resolved anisotropy measurements were consistent with PMP1 fragment immobilization within peptide-detergent complexes [7].

References

Zinc finger protein Prz1 regulates Ca2+ but not Cl- homeostasis in fission yeast. Identification of distinct branches of calcineurin signaling pathway in fission yeast. Hirayama, S., Sugiura, R., Lu, Y., Maeda, T., Kawagishi, K., Yokoyama, M., Tohda, H., Giga-Hama, Y., Shuntoh, H., Kuno, T. J. Biol. Chem. (2003) [Pubmed]
Two distinct genes encode small isoproteolipids affecting plasma membrane H(+)-ATPase activity of Saccharomyces cerevisiae. Navarre, C., Catty, P., Leterme, S., Dietrich, F., Goffeau, A. J. Biol. Chem. (1994) [Pubmed]
Purification and complete sequence of a small proteolipid associated with the plasma membrane H(+)-ATPase of Saccharomyces cerevisiae. Navarre, C., Ghislain, M., Leterme, S., Ferroud, C., Dufour, J.P., Goffeau, A. J. Biol. Chem. (1992) [Pubmed]
Deciphering the role of individual acyl chains in the interaction network between phosphatidylserines and a single-spanning membrane protein. Mousson, F., Coïc, Y.M., Baleux, F., Beswick, V., Sanson, A., Neumann, J.M. Biochemistry (2002) [Pubmed]
1H- and 2H-NMR studies of a fragment of PMP1, a regulatory subunit associated with the yeast plasma membrane H(+)-ATPase. Conformational properties and lipid-peptide interactions. Beswick, V., Roux, M., Navarre, C., Coïc, Y.M., Huynh-Dinh, T., Goffeau, A., Sanson, A., Neumann, J.M. Biochimie (1998) [Pubmed]
PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from bilayer mixtures with phosphatidylcholine: a (2)H-NMR study. Roux, M., Beswick, V., Coïc, Y.M., Huynh-Dinh, T., Sanson, A., Neumann, J.M. Biophys. J. (2000) [Pubmed]
Single-spanning membrane protein insertion in membrane mimetic systems: role and localization of aromatic residues. Coïc, Y.M., Vincent, M., Gallay, J., Baleux, F., Mousson, F., Beswick, V., Neumann, J.M., de Foresta, B. Eur. Biophys. J. (2005) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use

[search][advanced]