Abstract:
:Lipid rafts are specialized plasma membrane microdomains in which glycosphingolipids and cholesterol are major structural components. Their relative insolubility to nonionic detergents is the most widely used method to purify these structures. Several signalling proteins are associated with these microdomains in T lymphocytes, including receptors for growth factors and cytokines. ProTalpha is a highly conserved and widely distributed protein whose physiological functions remain elusive. In previous works we identified, by means of affinity cross-linking, affinity chromatography and fluorescence microscopy, a set of binding proteins for ProTalpha in human lymphoblasts. Now, this work goes deeply in that ProTalpha receptor description revealing, by different experimental approaches, its presence in lipid rafts. Moreover, our results fit a model in which a tyrosine phosphorylation signalling cascade confined to rafts is initiated upon ProTalpha receptor recognition, which represents an important and promising finding in the research for elucidating the molecular mechanisms underlying the immunomodulatory functions of ProTalpha.
journal_name
Mol Membr Bioljournal_title
Molecular membrane biologyauthors
Salgado FJ,Piñeiro A,Canda-Sánchez A,Lojo J,Nogueira Mdoi
10.1080/09687860500063506subject
Has Abstractpub_date
2005-05-01 00:00:00pages
163-76issue
3eissn
0968-7688issn
1464-5203pii
T168872277510356journal_volume
22pub_type
杂志文章abstract::That some membranes restrict certain lipid species to one side of the bilayer and others to the opposite side has been known for two decades. However, how this asymmetric transbilayer distribution is generated and controlled, how many and what type of membranes are so structured, and even the reason for its existence ...
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abstract::In Saccharomyces cerevisiae Jen1p is a lactate/proton symporter belonging to the lactate/pyruvate:H(+) symporter subfamily (TC#2.A.1.12.2) of the Major Facilitator Superfamily. We investigated structure-function relationships of Jen1p using a rational mutational analysis based on the identification of conserved amino ...
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