{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,5,14]],"date-time":"2024-05-14T11:15:19Z","timestamp":1715685319483},"reference-count":54,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2000,3,1]],"date-time":"2000-03-01T00:00:00Z","timestamp":951868800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2000,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Eukaryotic elongation factor 1\u03b1 (eEF1A) can be post-translationally modified by the addition of phosphorylglycerylethanolamine (PGE). [14C]Ethanolamine was incorporated into the PGE modification, and with carrot (Daucus carota L.) suspension culture cells, eEF1A was the only protein that incorporated detectable quantities of [14C]ethanolamine (Ransom et al., 1998). When 1 mm CaCl2 was added to microsomes containing [14C]ethanolamine-labeled eEF1A ([14C]et-eEF1A), there was a 60% decrease in the amount of [14C]et-eEF1A recovered after 10 min. The loss of endogenous [14C]et-eEF1A was prevented by adding EGTA. Recombinant eEF1A, which did not contain the PGE modification, also was degraded by microsomes in a Ca2+-regulated manner, indicating that PGE modification was not necessary for proteolysis; however, it enabled us to quantify enodgenous eEF1A. By monitoring [14C]et-eEF1A, we found that treatment with phospholipase D or C, but not phospholipase A2, resulted in a decrease in [14C]et-eEF1A from carrot microsomes. The fact that there was no loss of [14C]et-eEF1A with phospholipase A2 treatment even in the presence of 1 mmCa2+ suggested that the loss of membrane lipids was not essential for eEF1A proteolysis and that lysolipids or fatty acids decreased proteolysis. At micromolar Ca2+ concentrations, proteolysis of eEF1A was pH sensitive. When 1 \u03bcmCaCl2 was added at pH 7.2, 35% of [14C]et-eEF1A was lost; while at pH 6.8, 10 \u03bcm CaCl2 was required to give a similar loss of protein. These data suggest that eEF1A may be an important downstream target for Ca2+ and lipid-mediated signal transduction cascades.<\/jats:p>","DOI":"10.1104\/pp.122.3.957","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T05:01:20Z","timestamp":1027746080000},"page":"957-966","source":"Crossref","is-referenced-by-count":15,"title":["Calcium-Regulated Proteolysis of eEF1A"],"prefix":"10.1093","volume":"122","author":[{"given":"Wendy D.","family":"Ransom-Hodgkins","sequence":"first","affiliation":[{"name":"Botany Department, North Carolina State University, Raleigh, North Carolina 27695\u20137612 (W.D.R.-H., I.B., W.F.B.); and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Irena","family":"Brglez","sequence":"additional","affiliation":[{"name":"Botany Department, North Carolina State University, Raleigh, North Carolina 27695\u20137612 (W.D.R.-H., I.B., W.F.B.); and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xuemin","family":"Wang","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506 (X.W.)"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wendy F.","family":"Boss","sequence":"additional","affiliation":[{"name":"Botany Department, North Carolina State University, Raleigh, North Carolina 27695\u20137612 (W.D.R.-H., I.B., W.F.B.); and"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2000,3,1]]},"reference":[{"key":"2021062510385304400_R1","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/0014-5793(87)80848-7","article-title":"Cyclic AMP induces alkalinization in Dictyostelium.","volume":"220","author":"Aerts","year":"1987","journal-title":"FEBS 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