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Updated: Aug 20, 2026

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry
Published on: May 17, 2016
Profilin regulates the activity of p42POP, a novel Myb-related transcription factor
Marcell Lederer1, Brigitte M Jockusch, Martin Rothkegel
1Cell Biology, Zoological Institute, Technical University of Braunschweig, 38092 Braunschweig, Germany.
Abstract:
Profilins, regulators of cytoplasmic actin dynamics, also bind to several nuclear proteins but the significance of these interactions is mostly unclear. Here, we describe a novel Myb-related transcription factor, p42POP, as a new ligand for profilin and show that profilin regulates its activity. p42POP comprises a unique combination of domains and is widely expressed in mouse tissues. In contrast to many other Myb proteins, it contains only one functional tryptophan-cluster motif. This is followed by an acidic domain, a leucine zipper that mediates dimerization and functional nuclear import and export signals that can direct p42POP to either the nuclear or the cytoplasmic compartment. Binding to profilins is mediated by a proline-rich cluster. p42POP-profilin complexes can be precipitated from cell lysates. In transfected cells displaying p42POP in the nucleus, nuclear profilin is markedly increased. When p42POP is anchored at mitochondrial membranes, profilin is targeted to this location. Hence, in a cellular environment, p42POP and profilin are found in the same protein complex. In luciferase assays, p42POP acts as repressor and this activity is substantially reduced by profilins, indicating that profilin can regulate p42POP activity and is therefore involved in gene regulation.
Insights
Profilins bind to the novel Myb-related transcription factor p42POP, regulating its gene activity. This interaction influences p42POP
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Profilins regulate actin dynamics and interact with nuclear proteins.
- The functional significance of profilin-nuclear protein interactions remains largely unknown.
Purpose of the Study:
- To identify novel profilin ligands.
- To characterize the interaction between profilin and a new Myb-related transcription factor, p42POP.
- To elucidate profilin's regulatory role in p42POP activity and gene regulation.
Main Methods:
- Identification and characterization of p42POP, a novel Myb-related transcription factor.
- Analysis of p42POP domain structure, including proline-rich regions for profilin binding.
- Co-immunoprecipitation assays to detect p42POP-profilin complexes.
- Cellular localization studies of p42POP and profilin.
- Luciferase reporter assays to assess p42POP's transcriptional activity and profilin's regulatory effect.
Main Results:
- p42POP is a novel Myb-related transcription factor with a unique domain combination and wide tissue expression.
- Profilin binds to p42POP via a proline-rich cluster, forming cellular complexes.
- Profilin binding significantly reduces p42POP's repressor activity in gene regulation.
- p42POP influences the cellular localization of profilin, including targeting it to mitochondria.
Conclusions:
- Profilin acts as a regulator of the Myb-related transcription factor p42POP.
- The interaction between profilin and p42POP plays a role in modulating gene regulation.
- p42POP is a new cellular target for profilin, impacting its localization and function.
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