Rab5(Q79L) interacts with the carboxyl terminus of RUFY3

Yoshida, Hitomi; Okumura, Naoko; Shirafuji, Naoki; Matsuda, Satoru

doi:10.7150/ijbs.6.187

Cited by 15 publications

(16 citation statements)

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“…The Rab proteins are a large family of small GTPases that participate in regulating intracellular vesicular membrane trafficking pathways. Some Rab proteins recruit effectors to promote vesicle formation and membrane fusion and play a fundamental role in phagosome formation and early endocytic pathways [23,24]. For example, Rab8 plays an important role in exocytic membrane traffic from Golgi complex to plasma membrane [25].…”

Section: Small Gtpases Also Associate With Motor Proteins And/or Filamentioning

confidence: 99%

How do you RUN on?

et al. 2011

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a b s t r a c tRUN domain is present in several proteins related to the functions of Rap and Rab family GTPases. Accumulating evidence supports the hypothesis that RUN domain-containing proteins act as a component of vesicle traffic and might be responsible for an interaction with a filamentous network linked to actin cytoskeleton or microtubules. That is to say, on one hand, RUN domains associate with Rab or Rap family proteins, on the other hand, they also might interact with motor proteins such as kinesin or myosin via intervention molecules. In this review, we summarize the background and current status of RUN domain research with an emphasis on the interaction between RUN domain and motor proteins with respect to the vesicle traffic on filamentous network.

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Section: Small Gtpases Also Associate With Motor Proteins And/or Filamentioning

confidence: 99%

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et al. 2011

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“…RUFY3 also contains the RUN domain and seems to play important roles in multiple Ras-like GTPase signaling pathways 13 . Rab5 engages in a GTP-dependent interaction with RUFY3.…”

Section: Introductionmentioning

confidence: 99%

RUFY3 interaction with FOXK1 promotes invasion and metastasis in colorectal cancer

Xie

Wang

Liu

et al. 2017

Sci Rep

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RUFY3 is highly expressed in brain tissue and has a role in neuronal development. Transcriptional factor FOXK1 is involved in cell growth and metabolism. We knew that RUFY3 or FOXK1 has been correlated with the malignant of tumor cells. However, the role of these molecules in colorectal cancer (CRC) progression remains unknown. We investigated the protein expression levels by Western blot, immunofluorescence and immunohistochemistry analyses. The migration and invasive abilities of CRC cells were assessed using shRNA-mediated inhibition in vitro and in vivo. We showed that RUFY3 expression was up-regulated in CRC compared with its expression in a normal human colon cell line (FHC). RUFY3 suppression inhibited anchorage independent cell tumorigenesis. RUFY3 induced elevated expression of eight major oncogenes. Moreover, RUFY3 physically interacts with FOXK1 in CRC. A positive correlation was observed between the expression patterns of RUFY3 and FOXK1. Furthermore, RUFY3 and FOXK1 expression were correlated with tumor progression and represented significant predictors of overall survival in CRC patients. SiRNA-mediated repression of FOXK1 in RUFY3-overexpressing cells reversed the epithelial-mesenchymal transition (EMT) and metastatic phenotypes. In vivo, FOXK1 promoted RUFY3-mediated metastasis via orthotopic implantation. These findings suggest that the RUFY3-FOXK1 axis might promote the development and progression of human CRC.

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“…RUFY3 is distributed between the cytosol and at the plasma membrane, but not in intracellular vesicles, presumably because it lacks a FYVE domain. In artificial conditions, like following expression of the dominant gain of function mutant form of Rab5 (Q79L) in U937 cells, RUFY3 was found associated in large vesicle structures and to co-immunoprecipitate with Rab5, via an interaction with its carboxyl terminal domain and surprisingly not its RUN domain ( Yoshida et al, 2010 ). Like RUFY2, RUFY3 was also shown in a 2-hybrid screen and by co-immunoprecipitation to bind Rab33, through its coiled-coil domain 1 (CC1; Fukuda et al, 2011 ).…”

Section: Rufy3mentioning

confidence: 99%

The RUFYs, a Family of Effector Proteins Involved in Intracellular Trafficking and Cytoskeleton Dynamics

Char

Pierre

2020

Front. Cell Dev. Biol.

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Intracellular trafficking is essential for cell structure and function. In order to perform key tasks such as phagocytosis, secretion or migration, cells must coordinate their intracellular trafficking, and cytoskeleton dynamics. This relies on certain classes of proteins endowed with specialized and conserved domains that bridge membranes with effector proteins. Of particular interest are proteins capable of interacting with membrane subdomains enriched in specific phosphatidylinositol lipids, tightly regulated by various kinases and phosphatases. Here, we focus on the poorly studied RUFY family of adaptor proteins, characterized by a RUN domain, which interacts with small GTP-binding proteins, and a FYVE domain, involved in the recognition of phosphatidylinositol 3-phosphate. We report recent findings on this protein family that regulates endosomal trafficking, cell migration and upon dysfunction, can lead to severe pathology at the organismal level.

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Rab5(Q79L) interacts with the carboxyl terminus of RUFY3

Cited by 15 publications

References 9 publications

How do you RUN on?

How do you RUN on?

RUFY3 interaction with FOXK1 promotes invasion and metastasis in colorectal cancer

The RUFYs, a Family of Effector Proteins Involved in Intracellular Trafficking and Cytoskeleton Dynamics

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