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The L1TD1 protein interactome reveals the importance of post-transcriptional regulation in human pluripotency.

Emani MR, Närvä E, Stubb A, Chakroborty D, Viitala M, Rokka A, Rahkonen N, Moulder R, Denessiouk K, Trokovic R, Lund R, Elo LL, Lahesmaa R - Stem Cell Reports (2015)

Bottom Line: Our data reveal that L1TD1 has an important role in RNA splicing, translation, protein traffic, and degradation.L1TD1 interacts with multiple stem-cell-specific proteins, many of which are still uncharacterized in the context of development.Further, we show that L1TD1 is a part of the pluripotency interactome network of OCT4, SOX2, and NANOG, bridging nuclear and cytoplasmic regulation and highlighting the importance of RNA biology in pluripotency.

View Article: PubMed Central - PubMed

Affiliation: Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20521 Turku, Finland.

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L1TD1 Participates in the High Proteasome Activity of Pluripotency(A) WB detection of PSMD11 in L1TD1, IgG control, and UB IP reactions. hESC line HS360.(B) Protein expression of PSMD11 after L1TD1 silencing. hESC line HS360. NT, non-targeting. Quantifications can be found in the Supplemental Results.(C) Protein expression of L1TD1, OCT4, LIN28, SOX2, and GAPDH after inhibition of proteosomal activity with MG-132 inhibitor (10 μM) versus DMSO control. hESC line H9.
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fig3: L1TD1 Participates in the High Proteasome Activity of Pluripotency(A) WB detection of PSMD11 in L1TD1, IgG control, and UB IP reactions. hESC line HS360.(B) Protein expression of PSMD11 after L1TD1 silencing. hESC line HS360. NT, non-targeting. Quantifications can be found in the Supplemental Results.(C) Protein expression of L1TD1, OCT4, LIN28, SOX2, and GAPDH after inhibition of proteosomal activity with MG-132 inhibitor (10 μM) versus DMSO control. hESC line H9.

Mentions: The LC-MS/MS analysis resulted in the identification of multiple members of the ubiquitin-dependent proteasome, such as PSMD1, PSMD2, PSMD7, PSMD8, PSMD11, and PSMD14. Of particular interest, PSMD11 was recently reported to be responsible for the increased proteasome activity in hESCs, which is important for the maintenance of pluripotency (Vilchez et al., 2012). The interaction between L1TD1 and PSMD11 was validated with immunoblotting (Figure 3A). Moreover, silencing of L1TD1 resulted in decreased levels of PSMD11 (Figure 3B).


The L1TD1 protein interactome reveals the importance of post-transcriptional regulation in human pluripotency.

Emani MR, Närvä E, Stubb A, Chakroborty D, Viitala M, Rokka A, Rahkonen N, Moulder R, Denessiouk K, Trokovic R, Lund R, Elo LL, Lahesmaa R - Stem Cell Reports (2015)

L1TD1 Participates in the High Proteasome Activity of Pluripotency(A) WB detection of PSMD11 in L1TD1, IgG control, and UB IP reactions. hESC line HS360.(B) Protein expression of PSMD11 after L1TD1 silencing. hESC line HS360. NT, non-targeting. Quantifications can be found in the Supplemental Results.(C) Protein expression of L1TD1, OCT4, LIN28, SOX2, and GAPDH after inhibition of proteosomal activity with MG-132 inhibitor (10 μM) versus DMSO control. hESC line H9.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4376047&req=5

fig3: L1TD1 Participates in the High Proteasome Activity of Pluripotency(A) WB detection of PSMD11 in L1TD1, IgG control, and UB IP reactions. hESC line HS360.(B) Protein expression of PSMD11 after L1TD1 silencing. hESC line HS360. NT, non-targeting. Quantifications can be found in the Supplemental Results.(C) Protein expression of L1TD1, OCT4, LIN28, SOX2, and GAPDH after inhibition of proteosomal activity with MG-132 inhibitor (10 μM) versus DMSO control. hESC line H9.
Mentions: The LC-MS/MS analysis resulted in the identification of multiple members of the ubiquitin-dependent proteasome, such as PSMD1, PSMD2, PSMD7, PSMD8, PSMD11, and PSMD14. Of particular interest, PSMD11 was recently reported to be responsible for the increased proteasome activity in hESCs, which is important for the maintenance of pluripotency (Vilchez et al., 2012). The interaction between L1TD1 and PSMD11 was validated with immunoblotting (Figure 3A). Moreover, silencing of L1TD1 resulted in decreased levels of PSMD11 (Figure 3B).

Bottom Line: Our data reveal that L1TD1 has an important role in RNA splicing, translation, protein traffic, and degradation.L1TD1 interacts with multiple stem-cell-specific proteins, many of which are still uncharacterized in the context of development.Further, we show that L1TD1 is a part of the pluripotency interactome network of OCT4, SOX2, and NANOG, bridging nuclear and cytoplasmic regulation and highlighting the importance of RNA biology in pluripotency.

View Article: PubMed Central - PubMed

Affiliation: Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20521 Turku, Finland.

Show MeSH