Protein tyrosine phosphatase interacting protein 51—a jack-of-all-trades protein

Brobeil, Alexander; Bobrich, Manuel; Wimmer, Monika

doi:10.1007/s00441-011-1146-1

Cited by 16 publications

(42 citation statements)

References 68 publications

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“…Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a multifunctional protein with implication in processes like proliferation, differentiation and apoptosis [1,2]. To fulfill these opposite functions the PTPIP51 protein possesses different domains necessary for protein-protein interaction and subcellular localization [1,3,4].…”

Section: Introductionmentioning

confidence: 99%

“…To fulfill these opposite functions the PTPIP51 protein possesses different domains necessary for protein-protein interaction and subcellular localization [1,3,4]. …”

Section: Introductionmentioning

confidence: 99%

“…This protein family of microtubule associated proteins comprises three members, named RMD-1, RMD-2 and RMD-3 [1]. RMD-1 was identified to play a key role in mitogenic processes, especially in the correct segregation of the chromosomes during mitosis [11].…”

Section: Introductionmentioning

confidence: 99%

“…Yet, the exact mechanism of spindle assembly to the kinetochores remains elusive [12]. As has been revealed by co-immunoprecipitation experiments, PTPIP51 interacts with two mitotic proteins, namely CGI-99 and Nuf-2 [1,2]. …”

Section: Introductionmentioning

confidence: 99%

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Interaction of PTPIP51 with Tubulin, CGI-99 and Nuf2 During Cell Cycle Progression

et al. 2012

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Protein tyrosine phosphatase interacting protein 51 (PTPIP51), also known as regulator of microtubule dynamics protein 3, was identified as an in vitro and in vivo interaction partner of CGI-99 and Nuf-2. PTPIP51 mRNA is expressed in all stages of the cell cycle; it is highly expressed six hours post-nocodazole treatment and minimally expressed one hour post-nocodazole treatment. Recent investigations located PTPIP51 protein at the equatorial plate. This study reports the localization of the PTPIP51/CGI-99 and the PTPIP51/Nuf-2 complex at the equatorial region during mitosis. Moreover, Duolink proximity ligation assays revealed an association of PTPIP51 with the microtubular cytoskeleton and the spindle apparatus. High amounts of phosphorylated PTPIP51 associated with the spindle poles was seen by confocal microscopy. In parallel a strong interaction of PTPIP51 with the epidermal growth factor receptor phosphorylating PTPIP51 at the tyrosine 176 residue was seen. In the M/G1 transition a high level of interaction between PTPIP51 and PTP1B was registered, thus restoring the interaction of PTPIP51 and Raf-1, depleted in mitotic cells. Summarizing these new facts, we conclude that PTPIP51 is necessary for normal mitotic processes, impacting on chromosomal division and control of the MAPK pathway activity.

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Section: Introductionmentioning

confidence: 99%

“…To fulfill these opposite functions the PTPIP51 protein possesses different domains necessary for protein-protein interaction and subcellular localization [1,3,4]. …”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Interaction of PTPIP51 with Tubulin, CGI-99 and Nuf2 During Cell Cycle Progression

et al. 2012

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“…Transcriptomic analysis during rat retinal development enabled us to identify a protein tyrosine phosphatase interacting protein (PTPIP) named PTPIP51 -also called FAM82A2 or RMD-3 -whose mRNA expression is downregulated in post-natal retinal explants when photoreceptor differentiation is blocked (Roger et al, 2007). This protein was first identified by yeast two-hybrid screening as an interacting partner of two non-receptor protein tyrosine phosphatases, namely protein tyrosine phosphatase 1B and T cell protein tyrosine phosphatase (Stenzinger et al, 2009b;Brobeil et al, 2011). PTPIP51 is expressed in diverse tissues including some regions of the mouse central nervous system (Maerker et al, 2008;Koch et al, 2009) as well as in developing and adult mammalian tissue and human carcinomas (Stenzinger et al, 2005;Koch et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

The protein tyrosine phosphatase interacting protein 51 (PTPIP51) is required for the differentiation of photoreceptors

et al. 2015

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Proliferation and differentiation of retinal progenitor cells (RPCs) are tightly controlled by extrinsic cues and distinct combinations of transcription factors leading to the generation of retinal cell type diversity. In this context, we investigated the role of the protein tyrosine phosphatase interacting protein 51 (PTPIP51) in the differentiation of RPCs. The expression pattern of PTPIP51 was analyzed by immunostaining during post-natal retinal development in the rat. Ex vivo electroporation has been used to silence or misexpress PTPIP51 in post-natal retinal explants, and the retinal phenotype was investigated after 3-7days in vitro (div). PTPIP51 expression in the retina started postnatally and was maintained throughout adulthood, especially in retinal ganglion cells and in the inner segment of photoreceptor cells. Silencing of Ptpip51 expression in postnatal retina failed to modify the commitment of late RPCs in the different lineages but severely impaired the final differentiation of photoreceptors, observed by a decrease in the fraction of Rhodopsin-positive cells after 7div. By contrast, misexpression of PTPIP51 in early or late RPCs failed to modify the differentiation of the RPCs. Our data demonstrate that PTPIP51 is implicated in the differentiation process of immature photoreceptors. Because PTPIP51 is specifically localized in the inner segment, PTPIP51 may contribute to the complex stage of maturation of the apical segment of these cells.

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Orchestrating cellular signaling pathways—the cellular “conductor” protein tyrosine phosphatase interacting protein 51 (PTPIP51)

et al. 2016

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The protein tyrosine phosphatase interacting protein 51 (PTPIP51) is thought to regulate crucial cellular functions such as mitosis, apoptosis, migration, differentiation and communication between organelles as a scaffold protein. These diverse functions are modulated by the tyrosine/serine phosphorylation status of PTPIP51. This review interconnects the insights obtained about the action of PTPIP51 in mitogen-activated protein kinase signaling, nuclear factor kB signaling, calcium homeostasis and chromosomal segregation and identifies important signaling hubs. The interference of PTPIP51 in such multiprotein complexes and their PTPIP51-modulated cross-talk makes PTPIP51 an ideal target for novel drugs such as the small molecule LDC-3. Graphical Abstract ᅟ.

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Protein tyrosine phosphatase interacting protein 51—a jack-of-all-trades protein

Cited by 16 publications

References 68 publications

Interaction of PTPIP51 with Tubulin, CGI-99 and Nuf2 During Cell Cycle Progression

Interaction of PTPIP51 with Tubulin, CGI-99 and Nuf2 During Cell Cycle Progression

The protein tyrosine phosphatase interacting protein 51 (PTPIP51) is required for the differentiation of photoreceptors

Orchestrating cellular signaling pathways—the cellular “conductor” protein tyrosine phosphatase interacting protein 51 (PTPIP51)

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