Rybp interacts with Hippi and enhances Hippi-mediated apoptosis

Stanton, Sasha E.; Blanck, J. K.; Locker, Joseph; Schreiber‐Agus, Nicole

doi:10.1007/s10495-007-0131-3

Cited by 25 publications

(22 citation statements)

References 31 publications

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“…It remains to be found out whether HIP-1 also directly interacts with DNA. Role of other interacting partners of HIPPI, namely RYBP (29) and BAR (30) in the transcription regulation by HIPPI is also elusive.…”

Section: Discussionmentioning

confidence: 99%

Transcription regulation of caspase-1 by R393 of HIPPI and its molecular partner HIP-1

Banerjee

Datta

Majumder

et al. 2009

Nucleic Acids Research

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Earlier we have shown that exogenous expression of HIPPI, a molecular partner of Huntingtin interacting protein HIP-1, induces apoptosis and increases expression of caspases-1, -8 and -10 in HeLa and Neuro2A cells. The C-terminal pseudo death effector domain of HIPPI (pDED-HIPPI) specifically interacts with the putative promoter sequences of these genes. In the present manuscript, we predict from structural modeling of pDED-HIPPI that R393 of HIPPI is important for such interaction. R393E mutation in pDED-HIPPI decreases the interaction with the putative promoter of caspase-1 in cells. Expression of caspase-1 is decreased in cells expressing mutant pDED-HIPPI in comparison to that observed in cells expressing wild type pDED-HIPPI. Using HIP-1 knocked down cells as well as over expressing HIP-1 with mutation at its nuclear localization signal and other deletion mutations, we demonstrate that translocation of HIPPI to the nucleus is mediated by HIP-1 for the increased expression of caspase-1. HIPPI-HIP-1 heterodimer is detected in cytoplasm as well as in the nucleus and is associated with transcription complex in cells. Taking together, we are able to show the importance of R393 of HIPPI and the role of HIPPI-HIP-1 heterodimer in the transcription regulation of caspase-1.

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Section: Discussionmentioning

confidence: 99%

Transcription regulation of caspase-1 by R393 of HIPPI and its molecular partner HIP-1

Banerjee

Datta

Majumder

et al. 2009

Nucleic Acids Research

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“…We mentioned above that HIP‐1 and HIPPI together induce apoptosis [23,24]. Identification of additional proteins such as Homer1c/Homer1 [31], BAR/BFAR [32], RybP [33], BLOC1S2 [34] and apoptin [35] that interact with HIPPI further indicates that HIPPI may regulate apoptosis. Homer1c/Homer1 belongs to the homer family of proteins and is known to participate, in neuronal signaling.…”

Section: Hippi and Its Interacting Partners – Regulation Of Apoptosismentioning

confidence: 99%

Huntington’s disease: roles of huntingtin‐interacting protein 1 (HIP‐1) and its molecular partner HIPPI in the regulation of apoptosis and transcription

2008

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Huntingtin protein (Htt), whose mutation causes Huntington’s disease (HD), interacts with large numbers of proteins that participate in diverse cellular pathways. This observation indicates that wild‐type Htt is involved in various cellular processes and that the mutated Htt alters these processes in HD. The roles of these interacting proteins in HD pathogenesis remain largely unknown. In the present review, we present evidence that Htt‐interacting protein 1 (HIP‐1), an endocytic protein, together with its interacting partner HIPPI, regulates apoptosis and gene expression, both processes being implicated in HD. Further studies are necessary to establish whether the HIPPI–HIP‐1 complex or other interacting partners of HIPPI regulate apoptosis and gene expression that are relevant to HD.

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“…It binds to several apoptotic mediators and induces apoptosis [11–13]. Enforced expression of RYBP inhibits the growth of cancer cells, but has minimal effects on non-transformed cells [14].…”

Section: Introductionmentioning

confidence: 99%

RYBP predicts survival of patients with non-small cell lung cancer and regulates tumor cell growth and the response to chemotherapy

Voruganti

Qin

et al. 2015

Cancer Letters

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Ring1 and YY1 binding protein (RYBP) is a member of Polycomb group (PcG) proteins and regulates cell growth through both PcG-dependent and -independent mechanisms. Our initial study indicated that RYBP is down-regulated in human non-small cell lung cancer (NSCLC) tissues. The present study determined the molecular role of RYBP in the development of NSCLC. We systemically investigated the association between the RYBP expression and the survival of patients with NSCLC. We also carried out in vitro and in vivo studies to explore the molecular basis for the tumor suppressing role of RYBP in NSCLC. Our clinical results demonstrated that the RYBP mRNA and protein expressions were significantly down-regulated in NSCLC and significantly linked to the poor prognosis in NSCLC patients. The enforced expression of RYBP inhibited cell survival, induced apoptosis, and increase chemosensitivity in NSCLC cells; knockdown of RYBP showed the opposite effects. Moreover, adenoviral delivery of RYBP sensitized the NSCLC cells to chemotherapy in vivo. In addition, RYBP expression was induced by paclitaxel, the first-line chemotherapeutic agent for NSCLC. Our results reveal that RYBP inhibits the aggressiveness of NSCLC cells and downregulation of RYBP is associated with poor prognosis,, suggesting that RYBP could be developed as a biomarker and a novel target for therapy in patients with lung cancer.

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Rybp interacts with Hippi and enhances Hippi-mediated apoptosis

Cited by 25 publications

References 31 publications

Transcription regulation of caspase-1 by R393 of HIPPI and its molecular partner HIP-1

Transcription regulation of caspase-1 by R393 of HIPPI and its molecular partner HIP-1

Huntington’s disease: roles of huntingtin‐interacting protein 1 (HIP‐1) and its molecular partner HIPPI in the regulation of apoptosis and transcription

RYBP predicts survival of patients with non-small cell lung cancer and regulates tumor cell growth and the response to chemotherapy

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