Identification of the proteins interacting with neuroprotective peptide humanin in a yeast two-hybrid system

Maximov, Vadim; Arman, I.P.; Tarantul, V. Z.

doi:10.1134/s1022795406020141

Cited by 4 publications

(9 citation statements)

References 16 publications

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“…Previous research has shown interaction of HN with HSP90 and EF1α ( Maximov et al, 2006 ), proteins also present at the lysosomal membrane and known to participate in CMA ( Bandyopadhyay et al, 2008 , 2010 ). Coimmunoprecipitation (coIP) experiments in cells expressing GFP-HN show that HSP90 but not EF1α, a known CMA regulator ( Bandyopadhyay et al, 2010 ), can be precipitated with HN using the GFP antibody ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Humanin is an endogenous activator of chaperone-mediated autophagy

Gong

Tasset

Díaz

et al. 2017

Journal of Cell Biology

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Section: Resultsmentioning

confidence: 99%

Humanin is an endogenous activator of chaperone-mediated autophagy

Gong

Tasset

Díaz

et al. 2017

Journal of Cell Biology

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“…MPP8 had been initially characterized in association with a Ran, Ras-like nuclear small GTPase 3 and a neuroprotective peptide 4 by the two-hybrid analyses. Recently, MPP8 has been shown to interact with histone H3 methylated at lysine 9 (H3K9me1/2/3) - a modification associated with transcriptional repression – via its N-terminal chromodomain (Fig.…”

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confidence: 99%

Structural Insights for MPP8 Chromodomain Interaction with Histone H3 Lysine 9: Potential Effect of Phosphorylation on Methyl-Lysine Binding

Chang

Horton

Bedford

et al. 2011

Journal of Molecular Biology

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M phase phosphoprotein 8 (MPP8) harbors a N-terminal chromodomain and a C-terminal ankyrin repeat domain. MPP8, via its chromodomain, binds histone H3 peptide tri- or di-methylated at lysine 9 (H3K9me3/2) in submicromolar affinity. We determined the crystal structure of MPP8 chromodomain in complex with H3K9me3 peptide. MPP8 interacts with at least six histone H3 residues from glutamine 5 to serine 10, enabling its ability to distinguish lysine 9 containing peptide (QTARKS) from that of lysine 27 (KAARKS), both sharing the ARKS sequence. A partial hydrophobic cage with three aromatic residues (Phe59, Trp80, Tyr83) and one aspartate (Asp87) encloses the methylated lysine 9. MPP8 has been reported to be phosphorylated in vivo, including the cage residue Tyr83 and the succeeding Thr84 and Ser85. Modeling a phosphate group onto the side chain hydroxyl oxygen of Tyr83 suggests the negatively charged phosphate group could enhance the binding of positively charged methyl-lysine or create a regulatory signal by allowing or inhibiting binding of other protein(s).

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“…We conducted a yeast two‐hybrid screening for HN‐interacting proteins in hope to find a clue for the mechanisms that may implicate HN in lymphomagenesis. As a result, we identified seven HN‐interacting proteins: PSMA5; HSP90AA1; PPA; PRDX1; MPP8; EEF1A1, and TSFM . However, the screening did not reveal any potential HN receptors or HN‐interacting proteins found earlier by other research groups (Table ).…”

Section: Discussionmentioning

confidence: 74%

“…Earlier, we used the yeast two‐hybrid screening to identify MPP8 and six other proteins as potential HN‐binding proteins . This binding needed further confirmation because the MPP8 protein might be involved in cancer development through promoting cancer cell motility and invasion .…”

Section: Resultsmentioning

confidence: 99%

“…In order to clarify molecular mechanisms of HN biological effects, we identified a set of proteins that interact with HN in the yeast two‐hybrid system. MPP8 was among these proteins . MPP8 is specifically phosphorylated at threonine within an FTPLQ motif in M‐phase of cell cycle and, therefore, may be involved in a cell cycle progression .…”

Section: Introductionmentioning

confidence: 99%

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Humanin binds MPP8: mapping interaction sites of the peptide and protein

Maximov

Martynenko

Arman

et al. 2013

Journal of Peptide Science

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Humanin (HN), a 24-amino acid peptide encoded by the mitochondrial 16S rRNA gene, was discovered by screening a cDNA library from the occipital cortex of a patient with Alzheimer's disease (AD) for a protection factor against AD-relevant insults. Earlier, using the yeast two-hybrid system, we have identified the M-phase phosphoprotein 8 (MPP8) as a binding partner for HN. In the present work, we further confirmed interaction of HN with MPP8 in co-immunoprecipitation experiments and localized an MPP8-binding site in the region between 5 and 12 aa. of HN. We have also shown that an MPP8 fragment (residues 431-560) is sufficient to bind HN. Further studies on functional consequences of the interaction between the potential oncopetide and the oncoprotein may elucidate some aspects of the molecular mechanisms of carcinogenesis.

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Identification of the proteins interacting with neuroprotective peptide humanin in a yeast two-hybrid system

Cited by 4 publications

References 16 publications

Humanin is an endogenous activator of chaperone-mediated autophagy

Humanin is an endogenous activator of chaperone-mediated autophagy

Structural Insights for MPP8 Chromodomain Interaction with Histone H3 Lysine 9: Potential Effect of Phosphorylation on Methyl-Lysine Binding

Humanin binds MPP8: mapping interaction sites of the peptide and protein

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