FILIP1 CT pull-down
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive Plus
ORGANISM(S): Mus musculus
TISSUE(S): Skeletal Muscle Cell Line
DISEASE(S): Not Available
SUBMITTER: 
Friedel Drepper
LAB HEAD: Bettina Warscheid
PROVIDER: PXD008875 | Pride | 2022-06-06
REPOSITORIES: Pride
Dataset's files
primary
| Action | DRS | |||
|---|---|---|---|---|
| QEplus018193.dat | Other | |||
| QEplus018193.mzid.gz | Mzid | |||
| QEplus018193.mzid_QEplus018193.MGF | Mzid | |||
| QEplus018193.raw | Raw | |||
| QEplus018195.dat | Other |
Items per page: 5 1 - 5 of 9 |
Publications
Phosphoproteomics identifies dual-site phosphorylation in an extended basophilic motif regulating FILIP1-mediated degradation of filamin-C.
Reimann Lena L Schwäble Anja N AN Fricke Anna L AL Mühlhäuser Wignand W D WWD Leber Yvonne Y Lohanadan Keerthika K Puchinger Martin G MG Schäuble Sascha S Faessler Erik E Wiese Heike H Reichenbach Christa C Knapp Bettina B Peikert Christian D CD Drepper Friedel F Hahn Udo U Kreutz Clemens C van der Ven Peter F M PFM Radziwill Gerald G Djinović-Carugo Kristina K Fürst Dieter O DO Warscheid Bettina B
Communications biology 20200522 1
The PI3K/Akt pathway promotes skeletal muscle growth and myogenic differentiation. Although its importance in skeletal muscle biology is well documented, many of its substrates remain to be identified. We here studied PI3K/Akt signaling in contracting skeletal muscle cells by quantitative phosphoproteomics. We identified the extended basophilic phosphosite motif RxRxxp[S/T]xxp[S/T] in various proteins including filamin-C (FLNc). Importantly, this extended motif, located in a unique insert in Ig- ...[more]
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