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E2f3a and E2f3b Localization\nThe subcellular location of E2f isoforms has not to our knowledge been addressed before. E2f3a and E2f3b share 110 C-terminal amino acids that encode the NLS, DNA-binding, marked box, transactivation, and Rb-binding domains [16], yet they exhibit different subcellular distribution in developing retinal cells. E2f3a is both nuclear and cytoplasmic, but E2f3b is always nuclear. The unique 121- and six-residue N-termini of E2f3a and E2f3b, respectively, likely mediate this difference. This region in E2f1, E2f2, and E2f3a binds Ccna2, establishing a negative regulatory loop that deactivates E2fs in mid-late S-phase [64,65]. However, even E2f3b, which lacks this domain, binds and is regulated by Ccna2 [18], so the domain difference may not explain the unique distributions we observed. Rb family and Tfdp proteins can also determine E2f localization [20–22], and we found that a portion of both Rb and Tfdp1 proteins are cytoplasmic in retinal cells. Indeed, immunostaining revealed that Rb and E2f3 colocalize to SAC processes.\nThe nuclear localization of E2f3b contrasts with that of other repressive E2fs in differentiating muscle, where E2f5 switches from the nucleus to cytoplasm, while E2f4 remains in both compartments [23]. The distinct compartmentalization of E2f3a and E2f3b in the retina suggests temporally and functionally distinct activities. Rb distribution matches that of E2f3a, consistent with its critical role in supporting SAC differentiation through E2f3a."}

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E2f3a and E2f3b Localization\nThe subcellular location of E2f isoforms has not to our knowledge been addressed before. E2f3a and E2f3b share 110 C-terminal amino acids that encode the NLS, DNA-binding, marked box, transactivation, and Rb-binding domains [16], yet they exhibit different subcellular distribution in developing retinal cells. E2f3a is both nuclear and cytoplasmic, but E2f3b is always nuclear. The unique 121- and six-residue N-termini of E2f3a and E2f3b, respectively, likely mediate this difference. This region in E2f1, E2f2, and E2f3a binds Ccna2, establishing a negative regulatory loop that deactivates E2fs in mid-late S-phase [64,65]. However, even E2f3b, which lacks this domain, binds and is regulated by Ccna2 [18], so the domain difference may not explain the unique distributions we observed. Rb family and Tfdp proteins can also determine E2f localization [20–22], and we found that a portion of both Rb and Tfdp1 proteins are cytoplasmic in retinal cells. Indeed, immunostaining revealed that Rb and E2f3 colocalize to SAC processes.\nThe nuclear localization of E2f3b contrasts with that of other repressive E2fs in differentiating muscle, where E2f5 switches from the nucleus to cytoplasm, while E2f4 remains in both compartments [23]. The distinct compartmentalization of E2f3a and E2f3b in the retina suggests temporally and functionally distinct activities. Rb distribution matches that of E2f3a, consistent with its critical role in supporting SAC differentiation through E2f3a."}

{"project":"craft-ca-core-dev","denotations":[{"id":"T25603","span":{"begin":9,"end":14},"obj":"PR:000028775"},{"id":"T25604","span":{"begin":70,"end":78},"obj":"SO:0001060"},{"id":"T25605","span":{"begin":127,"end":132},"obj":"PR:000028775"},{"id":"T25606","span":{"begin":192,"end":195},"obj":"SO:0001528"},{"id":"T25607","span":{"begin":243,"end":245},"obj":"PR:000013773"},{"id":"T25608","span":{"begin":254,"end":261},"obj":"SO:0000417"},{"id":"T25609","span":{"begin":334,"end":341},"obj":"UBERON:0000966"},{"id":"T25610","span":{"begin":334,"end":347},"obj":"CL:0009004"},{"id":"T25611","span":{"begin":349,"end":354},"obj":"PR:000028775"},{"id":"T25612","span":{"begin":363,"end":370},"obj":"GO:0005634"},{"id":"T25613","span":{"begin":375,"end":386},"obj":"GO:0005737"},{"id":"T25614","span":{"begin":408,"end":415},"obj":"GO:0005634"},{"id":"T25615","span":{"begin":462,"end":467},"obj":"PR:000028775"},{"id":"T25616","span":{"begin":540,"end":544},"obj":"PR:000006852"},{"id":"T25617","span":{"begin":546,"end":550},"obj":"PR:000006853"},{"id":"T25618","span":{"begin":556,"end":561},"obj":"PR:000028775"},{"id":"T25619","span":{"begin":568,"end":573},"obj":"PR:000005115"},{"id":"T25620","span":{"begin":649,"end":656},"obj":"GO:0051320"},{"id":"T25621","span":{"begin":704,"end":710},"obj":"SO:0000417"},{"id":"T25622","span":{"begin":725,"end":734},"obj":"GO:0065007"},{"id":"T25623","span":{"begin":738,"end":743},"obj":"PR:000005115"},{"id":"T25624","span":{"begin":757,"end":763},"obj":"SO:0000417"},{"id":"T25625","span":{"begin":829,"end":831},"obj":"PR:000013773"},{"id":"T25626","span":{"begin":938,"end":940},"obj":"PR:000013773"},{"id":"T25627","span":{"begin":945,"end":950},"obj":"PR:000016269"},{"id":"T25628","span":{"begin":964,"end":975},"obj":"GO:0005737"},{"id":"T25629","span":{"begin":979,"end":986},"obj":"UBERON:0000966"},{"id":"T25630","span":{"begin":979,"end":992},"obj":"CL:0009004"},{"id":"T25631","span":{"begin":1031,"end":1033},"obj":"PR:000013773"},{"id":"T25632","span":{"begin":1038,"end":1042},"obj":"PR:000006854"},{"id":"T25633","span":{"begin":1061,"end":1070},"obj":"GO:0042995"},{"id":"T25634","span":{"begin":1076,"end":1083},"obj":"GO:0005634"},{"id":"T25635","span":{"begin":1184,"end":1188},"obj":"PR:000006856"},{"id":"T25636","span":{"begin":1207,"end":1214},"obj":"GO:0005634"},{"id":"T25637","span":{"begin":1218,"end":1227},"obj":"GO:0005737"},{"id":"T25638","span":{"begin":1235,"end":1239},"obj":"PR:000006855"},{"id":"T25639","span":{"begin":1312,"end":1317},"obj":"PR:000028775"},{"id":"T25640","span":{"begin":1335,"end":1341},"obj":"UBERON:0000966"},{"id":"T25641","span":{"begin":1400,"end":1402},"obj":"PR:000013773"},{"id":"T25642","span":{"begin":1432,"end":1437},"obj":"PR:000028775"},{"id":"T25643","span":{"begin":1515,"end":1520},"obj":"PR:000028775"}],"text":"Distinct E2f3a and E2f3b Localization\nThe subcellular location of E2f isoforms has not to our knowledge been addressed before. E2f3a and E2f3b share 110 C-terminal amino acids that encode the NLS, DNA-binding, marked box, transactivation, and Rb-binding domains [16], yet they exhibit different subcellular distribution in developing retinal cells. E2f3a is both nuclear and cytoplasmic, but E2f3b is always nuclear. The unique 121- and six-residue N-termini of E2f3a and E2f3b, respectively, likely mediate this difference. This region in E2f1, E2f2, and E2f3a binds Ccna2, establishing a negative regulatory loop that deactivates E2fs in mid-late S-phase [64,65]. However, even E2f3b, which lacks this domain, binds and is regulated by Ccna2 [18], so the domain difference may not explain the unique distributions we observed. Rb family and Tfdp proteins can also determine E2f localization [20–22], and we found that a portion of both Rb and Tfdp1 proteins are cytoplasmic in retinal cells. Indeed, immunostaining revealed that Rb and E2f3 colocalize to SAC processes.\nThe nuclear localization of E2f3b contrasts with that of other repressive E2fs in differentiating muscle, where E2f5 switches from the nucleus to cytoplasm, while E2f4 remains in both compartments [23]. The distinct compartmentalization of E2f3a and E2f3b in the retina suggests temporally and functionally distinct activities. Rb distribution matches that of E2f3a, consistent with its critical role in supporting SAC differentiation through E2f3a."}

{"project":"2_test","denotations":[{"id":"17608565-10779352-84869025","span":{"begin":263,"end":265},"obj":"10779352"},{"id":"17608565-8033208-84869026","span":{"begin":658,"end":660},"obj":"8033208"},{"id":"17608565-7969176-84869027","span":{"begin":661,"end":663},"obj":"7969176"},{"id":"17608565-11980909-84869028","span":{"begin":745,"end":747},"obj":"11980909"},{"id":"17608565-9144196-84869029","span":{"begin":894,"end":896},"obj":"9144196"},{"id":"17608565-9271426-84869029","span":{"begin":894,"end":896},"obj":"9271426"},{"id":"17608565-9372959-84869029","span":{"begin":894,"end":896},"obj":"9372959"},{"id":"17608565-10725332-84869030","span":{"begin":1270,"end":1272},"obj":"10725332"},{"id":"T70038","span":{"begin":263,"end":265},"obj":"10779352"},{"id":"T93814","span":{"begin":658,"end":660},"obj":"8033208"},{"id":"T18238","span":{"begin":661,"end":663},"obj":"7969176"},{"id":"T97278","span":{"begin":745,"end":747},"obj":"11980909"},{"id":"T66114","span":{"begin":894,"end":896},"obj":"9144196"},{"id":"T4989","span":{"begin":894,"end":896},"obj":"9271426"},{"id":"T40985","span":{"begin":894,"end":896},"obj":"9372959"},{"id":"T9363","span":{"begin":1270,"end":1272},"obj":"10725332"}],"text":"Distinct E2f3a and E2f3b Localization\nThe subcellular location of E2f isoforms has not to our knowledge been addressed before. E2f3a and E2f3b share 110 C-terminal amino acids that encode the NLS, DNA-binding, marked box, transactivation, and Rb-binding domains [16], yet they exhibit different subcellular distribution in developing retinal cells. E2f3a is both nuclear and cytoplasmic, but E2f3b is always nuclear. The unique 121- and six-residue N-termini of E2f3a and E2f3b, respectively, likely mediate this difference. This region in E2f1, E2f2, and E2f3a binds Ccna2, establishing a negative regulatory loop that deactivates E2fs in mid-late S-phase [64,65]. However, even E2f3b, which lacks this domain, binds and is regulated by Ccna2 [18], so the domain difference may not explain the unique distributions we observed. Rb family and Tfdp proteins can also determine E2f localization [20–22], and we found that a portion of both Rb and Tfdp1 proteins are cytoplasmic in retinal cells. Indeed, immunostaining revealed that Rb and E2f3 colocalize to SAC processes.\nThe nuclear localization of E2f3b contrasts with that of other repressive E2fs in differentiating muscle, where E2f5 switches from the nucleus to cytoplasm, while E2f4 remains in both compartments [23]. The distinct compartmentalization of E2f3a and E2f3b in the retina suggests temporally and functionally distinct activities. Rb distribution matches that of E2f3a, consistent with its critical role in supporting SAC differentiation through E2f3a."}