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090 _aB-12807
245 1 0 _aHydrophobic-Domain-Dependent Protein-Protein Interactions Mediate the Localization of GPAT Enzymes to ER Subdomains
490 0 _vTraffic, 12(4), p.452-472, 2011
520 3 _aThe endoplasmic reticulum (ER)is a dynamic organelle that consists of numerous regions or 'subdomains' that have discrete morphological features and functional properties. Although it is generally accepted that these subdomains differ in their protein and perhaps lipid compositions, a clear understanding of how they are assembled and maintained has not been well established. Wepreviously demonstrated that twodiacylglycerol acyltransferase enzymes (DGAT1 and DGAT2)from tung tree (Vernicia fordii ) were located in different subdomains of ER, but the mechanisms responsible for protein targeting to these subdomains were not elucidated. Here we extend these studies by describing two glycerol- 3-phosphate acyltransferase-like (GPAT)enzymes from tung tree, GPAT8 and GPAT9, that both colocalize with DGAT2 in the same ER subdomains.Measurement of protein- protein interactions using the split-ubiquitin assay revealed that GPAT8 interacts with itself, GPAT9 and DGAT2, but not with DGAT1. Furthermore, mutational analysis of GPAT8 revealed that the protein's first predicted hydrophobic region, which contains an amphipathic helix-like motif, is required for interaction with DGAT2 and for DGAT2-dependent colocalization in ER subdomains. Taken together, these results suggest that the regulation and organization of ER subdomains is mediated at least in part by higher-ordered, hydrophobicdomain- dependent homo- and hetero-oligomeric protein- protein interactions.
650 1 4 _aDIACYLGLYCEROL ACYLTRANSFERASE
650 1 4 _aENDOPLASMIC RETICULUM
650 1 4 _aGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE
650 1 4 _aPROTEIN-PROTEIN INTERACTIONS
650 1 4 _aPROTEIN TARGETING
650 1 4 _aPROTEIN TOPOLOGY
650 1 4 _aSUBDOMAIN
700 1 2 _aGidda, S.K.
700 1 2 _aShockey, J.M.
700 1 2 _aFalcone, M.
700 1 2 _aKim, P.K.
700 1 2 _aRothstein, S.J.
700 1 2 _aAndrews, D.W.
700 1 2 _aDyer, J.M.
700 1 2 _aDyer, J.M.
856 4 0 _uhttps://drive.google.com/file/d/1o_iB6eEqAvkAxPwTX8KiYKWebc_GwYQV/view?usp=drivesdk
_zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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