Abstract
The retromer is a multiprotein complex conserved from yeast to humans, which is involved in intracellular protein trafficking and protein recycling. Selection of cargo proteins transported by the retromer depends on the core retromer subunit composed of the three vacuolar protein sorting (VPS) proteins, namely VPS26, VPS29, and VPS35. To gain a better knowledge of the importance of the plant retromer in protein sorting, we carried out a comparative proteomic and metabolomic analysis of Arabidopsis thaliana seeds from the wild-type and the null-retromer mutant vps29. Here, we report that the retromer mutant displays major alterations in the maturation of seed storage proteins and synthesis of lipid reserves, which are accompanied by severely impaired seed vigor and longevity. We also show that the lack of retromer components is counterbalanced by an increase in proteins involved in intracellular trafficking, notably members of the Ras-related proteins in brain (RAB) family proteins. Our study suggests that loss of the retromer stimulates energy metabolism, affects many metabolic pathways, including that of cell wall biogenesis, and triggers an osmotic stress response, underlining the importance of retromer function in seed biology.
Highlights
The success of plant reproduction through the production of seeds depends on the proper accumulation of seed storage reserves that will enable germination and early seedling development [1]
Seed Germination and Longevity: An Integrative View Based on vps29 Proteomics and Metabolomics
Previous studies demonstrated that vacuolar sorting receptor (VSR) proteins are associated with germination success and seedling establishment, suggesting that deposition on storage proteins in protein storage vacuoles (PSVs) during seed development is important for seed vigor [28,29]
Summary
The success of plant reproduction through the production of seeds depends on the proper accumulation of seed storage reserves that will enable germination and early seedling development [1]. Vacuolar sorting receptors (VSRs) are involved in the maturation process as they transport proteolytic enzymes required for SSP maturation from the TGN to the PSV and lytic vacuole These receptors, such as AtVSR1/AtELP, are recycled to the TGN by a mechanism implicating the retromer complex [9]. In Arabidopsis, a pioneer study showed that VPS29 plays a key role in cell polarity and organ initiation [15], is required for the efficient sorting of seed storage proteins [9,16], and is required for the biogenesis and degradation of oil bodies [17]. We investigated the impact of the vps knockout mutation, which leads to the complete loss of retromer function [15], on seed physiology. Gel-Based Proteomics between Col-0 and vps Dry Mature Seeds 2.2. Gel-Based Proteomics between Col-0 and vps Dry Mature Seeds (pptitaavfipppp(mFhhnsobnpararrrhieevroooousrdgtamo2ttetiptttnugiemeeee9wsβcTrTsderritoiiuenoepn-nninoasomcgsalssasena2fiuufmnai,ceincrf)fnrwtb1cast.irdeaesnasdu2oufloIosdetyr.taSdnmcfuntrarosnherTcerimcuifttedtonasooodhrhasttc.nttueurrtesredihipa(motyoocBt“s1iawaolmivnnαihe2firmsm(pneesicaSo”ses[tlororaeid9ocharwpisbcilsudt]tnno-duiarecl,ustntsewusichrybiywFraesbitccaplie[irnzoelneig2lvunheeefuosf2iupeppgdinefpfes,1srgrre2actees2ir2eaifhlbsr7nideoor9uSedme2e]yadsisntx:etnraeipmpsr(epswstoii,F,orhmbatnalene“khtiamerbe)esghcβ“nia,tertxunuuiheeepapg”ofcpanirrerrnre”u2nwsbsleoidedseaDngoliudamcenaa2npirβuEnnniedrn)FasFt.i-draidecaisroradsnIsiglfeuoaatgunpnyogretubntfpuyerbascreoaterocnitthrludnderfssiyeetmtoiemon.edesimi2bo2rnoonifwiBasamtaysfemnpdste,t,ciatudbobh2cail(htten(dvrsna))oesDiese,.ertdhe-uthhesαcteErmoiAstyeodahrncssh,-ewoepeitwsaasaletediuueoenjyvntnndonedghbwpgpssdxrishsuoestenieehpehts2nfenpes2oyrtwef9edsdiorDrifr1scatenorasetraisi2tbEeaohs,atmregpSt(deumtlegrdhgseorkhieenhenoepe,geneesppdo“ltvrpyeao-pe2r“fhβwaebpprboowoDpoanc”yosaaurntmutf2”csstnEemirtneenti9erieaieiohnisnaddstrntnoFsoloenneaofofpestmirFdrasnmhgg,efbbrailcrusoidaywgym1eousboeuttr2sustoteuyeueiechioSoarfmorcshrgone2f“feoαma2cdhrpaαttarntD2c-,mhte,iiuas”hbahtcwoateE2iacs,s1e)eairnnbDi,.inem.2cerfnd)AateTaSd[Eaim,Feean9nrocnβsαiddcji]dvtiugtond,gr-ene-aeusrtutsasxwerlhaasuuricssppls[tnzhee-betitboi2reblfooegtiuot22uolec,pgadrrhuaa,wrnttnaash2aterebiw,ibeeiggnb7ieeeidtltdddnyse])eeeessrr,:,. Tmheetmabeotalobmoloicmaipcparpoparcohaclhedletdo ttohethqeuqaunatniftiicfiactaiotinonofof114433mmeetatabbooliltiteess,,aammoonngg wwhhiicchh tthhee aabbuunnddaanncceeooff 7k7W5-5swaawmlelirepserlkese-isgssaitngemisnfitpic,falipecnsavtnltayetllusaytel,tape
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