Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel member of the LIM protein gene family.
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The original cloning study identified LPP as the chromosome 3-derived partner of HMGIC/HMGA2 in lipoma and defined a proline-rich protein with three C-terminal LIM domains.
"Nucleotide sequence analysis of a composite cDNA of LPP revealed an open reading frame of 1836 nucleotides encoding a proline-rich protein containing a leucine-zipper motif in its amino-terminal region and three LIM domains in its carboxy-terminal region."
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The tumor-derived fusion transcripts retain either two or three LPP LIM domains, so these are rearrangement products rather than evidence for normal LPP isoform-specific functions.
"Two alternative HMGIC/LPP hybrid transcripts have been detected; the difference between them is mainly the presence of either two or three LIM domains in the predicted HMGI-C/LPP fusion proteins."
LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity.
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Human LPP localizes to focal adhesions and cell-cell contacts and binds VASP.
"LPP localizes in focal adhesions as well as in cell-to-cell contacts, and it binds VASP, a protein implicated in the control of actin organization."
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Leptomycin-B trapping and mutational analysis support CRM1-dependent nuclear export through an N-terminal leucine-rich export sequence.
"The nuclear export of LPP depends on an N-terminally located leucine-rich sequence that shares sequence homology with well-defined nuclear export signals."
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LPP has transcriptional activation capacity in a heterologous GAL4 reporter assay, which supports nuclear signaling potential but does not identify an endogenous target gene.
"Moreover, LPP displays transcriptional activation capacity, as measured by GAL4-based assays."
Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23).
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A secondary AML case carried reciprocal KMT2A/MLL-LPP fusion transcripts, with the predicted MLL-LPP product retaining the two last LPP LIM domains.
"The predicted MLL-LPP fusion protein includes the A/T hook motifs and methyltransferase domain of MLL joined to the two last LIM domains of LPP."
The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein.
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The three LPP LIM domains cooperate in robust focal-adhesion targeting, with a pivotal contribution from the LIM1-LIM2 linker.
"All of the LIM domains of LPP cooperate in order to provide robust targeting to focal adhesions, and the linker between LIM domains 1 and 2 plays a pivotal role in this targeting."
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The proline-rich region contains separable focal-adhesion and stress-fiber targeting information beyond its α-actinin- and VASP-binding sites.
"The proline-rich region of LPP contains targeting sites for focal adhesions and stress fibers that are distinct from the alpha-actinin and VASP binding sites, and the LPP LIM domains are dispensable for targeting LPP to the nucleus."
The lipoma preferred partner LPP interacts with alpha-actinin.
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Direct and cellular interaction assays map LPP binding to the central spectrin-repeat rod of α-actinin and to a conserved N-terminal LPP motif.
"This site was mapped to the central rod of alpha-actinin, which contains spectrin-like repeats 2 and 3. In the case of LPP, a conserved motif present at the N-terminus was shown to be responsible for the interaction."
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LPP binds α-actinin more weakly than zyxin in the quantitative two-/three-hybrid assays, limiting simple transfer of zyxin interaction behavior to LPP.
"Quantitative data obtained with the two-hybrid and the three-hybrid system suggest that LPP has a lower affinity for alpha-actinin than zyxin."
The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus.
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Scrib is a direct LPP partner, with binding mediated by Scrib PDZ domains and the LPP C terminus.
"The binding between Scrib and LPP is mediated by the PDZ domains of Scrib and the carboxy-terminus of LPP."
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In MDCKII and CV-1 cells, both proteins occupy cell-cell contacts, but Scrib is not required to target LPP to either focal adhesions or cell-cell contacts.
"Furthermore, our investigations indicate that Scrib is dispensable for targeting LPP to focal adhesions and to cell-cell contacts, and that LPP is not necessary for localizing Scrib in cell-cell contacts."
Angiotensin II, focal adhesion kinase, and PRX1 enhance smooth muscle expression of lipoma preferred partner and its newly identified binding partner palladin to promote cell migration.
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Palladin binds the first two LPP LIM domains through its N terminus in yeast-two-hybrid, in-vitro, and cellular assays.
"The palladin interacting region of LPP was mapped to the first and second LIM domains. The N-terminus of palladin interacted with LPP both in vitro and in vivo, but not solely through its FPLPPP and FPPPP motifs."
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LPP and palladin promote smooth-muscle-cell migration and spreading, with expression responsive to FAK, PRX1, angiotensin II, actin dynamics, and vascular injury.
"Both LPP and palladin enhanced cell migration and spreading."
Smooth muscle expression of lipoma preferred partner is mediated by an alternative intronic promoter that is regulated by serum response factor/myocardin.
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An intron-2 alternative promoter drives smooth-muscle-enriched LPP transcription and is directly regulated by SRF/myocardin.
"Quantitative RT-PCR shows that this alternative promoter directs transcription specifically to smooth muscle containing tissues in vivo."
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The alternative promoter is transcriptionally active in an SRF/myocardin- and CArG-box-dependent reporter assay.
"In reporter experiments, we show that the alternative promoter has transcriptional capacity that is dependent on SRF/myocardin and that the promoter associated CArG box is required for that activity."
Mechanical properties of the extracellular matrix alter expression of smooth muscle protein LPP and its partner palladin; relationship to early atherosclerosis and vascular injury.
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Rat R518 aortic smooth-muscle cells on denatured collagen or a rigid substrate up-regulate LPP and palladin together with pFAK and robust stress fibers.
"SMCs cultured on denatured collagen or on a rigid substrate, up regulated expression of LPP, its partner palladin, tenascin C (TN-C), phosphorylated focal adhesion kinase (pFAK) and exhibited robust stress fibers."
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LPP/palladin abundance is context-dependent across rat R518 substrate and oxidative-stress assays, human HIVS-125 endothelial/smooth-muscle co-culture flow, ApoE-null mouse atherosclerosis, and Sprague-Dawley rat vascular injury.
"In conclusion, expression of LPP and palladin are modulated by a mix of mechanical cues, oxidative stress and substrate composition which translate into their up or down regulation in vessel wall injury and early atherogenesis."
Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation.
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The seeded HDA source is a broad human fibroblast focal-adhesion proteomics dataset in which protein abundance was compared with and without myosin-II inhibition.
"We identified 905 focal adhesion proteins, 459 of which changed in abundance with myosin II inhibition, defining the myosin-II-responsive focal adhesion proteome."
A complex containing LPP and α-actinin mediates TGFβ-induced migration and invasion of ErbB2-expressing breast cancer cells.
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In human HER2-positive HCC1954 breast-cancer cells, transient LPP knockdown abolishes the TGFβ-induced increase in migration and invasion.
"Transient knockdown of LPP was sufficient to ablate the TGFβ-induced increase in migration (Fig. 1D) and invasion (Fig. 1E) seen in HCC1954 cells transfected with control siRNAs."
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In mouse NMuMG-ErbB2 breast-cancer cells, TGFβ drives Lpp recruitment to focal adhesions and Lpp-dependent focal-adhesion turnover.
"We show that LPP re-localizes to focal adhesion complexes upon TGFβ stimulation and is a critical determinant in TGFβ-mediated focal adhesion turnover."
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In mouse NMuMG-ErbB2 cells, an intact alpha-actinin-binding domain in Lpp is required for the TGFβ-induced migration and invasion phenotype.
"Taken together, these data demonstrate that the ability of LPP to promote TGFβ-induced migration and invasion requires its interaction with α-Actinin at focal adhesions."
Characterisation of Lipoma-Preferred Partner as a Novel Mechanotransducer in Vascular Smooth Muscle Cells.
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Mouse Lpp-null aortic VSMCs proliferate and invade more in culture, while native mesenteric arteries specifically show attenuated pressure-induced myogenic responses without loss of agonist-evoked contraction.
"In contrast, the myogenic response of LPP-KO MA segments was significantly attenuated while zyxin-deficient MA segments displayed a normal myogenic response."
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Mechanical stretch redistributes LPP toward stress fibers and the nucleus in mouse VSMCs.
"In response to stretching, LPP redistributed towards stress fibres and the nucleus."