The Ran binding protein RanBPM interacts with Axl and Sky receptor tyrosine kinases

Hafizi, Sassan; Gustafsson, Anna; Stenhoff, Jonas; Dahlbäck, Björn

doi:10.1016/j.biocel.2005.05.006

Cited by 39 publications

(32 citation statements)

References 38 publications

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“…It is this pool that is likely to be most relevant for Sema3A/ NRP1/PlexA signaling. RanBPM has been shown to interact with other plasma membrane proteins, suggesting a large role in mediating cell growth and signaling (Wang et al, 2002;Denti et al, 2004;Cheng et al, 2005;Hafizi et al, 2005). Because both MICAL and RanBPM have been implicated in integrin-based cellular responses to the extracellular matrix (Suzuki et al, 2002;Denti et al, 2004), both proteins provide potential sites for cross-talk between Sema3-dependent and matrixdependent regulation of axonal growth.…”

Section: Discussionmentioning

confidence: 99%

RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors

Togashi¹,

Schmidt²,

Strittmatter³

2006

J. Neurosci.

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Section: Discussionmentioning

confidence: 99%

RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors

Togashi¹,

Schmidt²,

Strittmatter³

2006

J. Neurosci.

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“…Importantly, all three of these SFKs are highly expressed in tissues of the central nervous system where they are likely to be found colocalized with Tyro-3. Yeast two-hybrid studies identified a number of proteins that potentially interact with Tyro-3, including RanBPM, protein phosphatase 1 (PP1), and the p85 β-subunit of PI3K (Hafizi et al, 2005a;Lan et al, 2000). Sequencing of the DNAs encoding the interacting proteins demonstrated that PI3K binds Tyro-3 via one of its SH2 domains and the interaction was confirmed in vitro and in vivo by GST pull-down assay and coimmunoprecipitation, respectively.…”

Section: Tyro-3 Signaling-thementioning

confidence: 99%

TAM Receptor Tyrosine Kinases: Biologic Functions, Signaling, and Potential Therapeutic Targeting in Human Cancer

Linger¹,

Keating²,

Earp

et al. 2008

Advances in Cancer Research

607

688

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Tyro-3, Axl, and Mer constitute the TAM family of receptor tyrosine kinases (RTKs) characterized by a conserved sequence within the kinase domain and adhesion molecule-like extracellular domains. This small family of RTKs regulates an intriguing mix of processes, including cell proliferation/survival, cell adhesion and migration, blood clot stabilization, and regulation of inflammatory cytokine release. Genetic or experimental alteration of TAM receptor function can contribute to a number of disease states, including coagulopathy, autoimmune disease, retinitis pigmentosa, and cancer. In this chapter, we first provide a comprehensive review of the structure, regulation, biologic functions, and down-stream signaling pathways of these receptors. In addition, we discuss recent evidence which suggests a role for TAM receptors in oncogenic mechanisms as family members are over-expressed in a spectrum of human cancers and have prognostic significance in some. Possible strategies for targeted inhibition of the TAM family in the treatment of human cancer are described. Further research will be necessary to evaluate the full clinical implications of TAM family expression and activation in cancer.

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“…Protein interaction algorithms suggested that LRP-1 and AXL do not directly bind each other, so we hypothesized the presence of a scaffolding protein. Further database searching indicated that the protein RANBP9 interacts with AXL in cancer cells (25) and with LRP-1 in neuronal cells (26). Although RANBP9 has not previously been implicated in any functional interaction between AXL and LRP-1 or in efferocytosis, we considered the hypothesis that it can act as an AXL/LRP-1 scaffolding protein in DCs to couple AXL-mediated AC binding with LRP-1-mediated AC internalization.…”

Section: Ranbp9 Facilitates the Functional Interaction Of Axl And Lrpmentioning

confidence: 99%

An AXL/LRP-1/RANBP9 complex mediates DC efferocytosis and antigen cross-presentation in vivo

Subramanian¹,

Hayes²,

Thome³

et al. 2014

J. Clin. Invest.

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The phagocytosis of apoptotic cells (ACs), or efferocytosis, by DCs is critical for self-tolerance and host defense. Although many efferocytosis-associated receptors have been described in vitro, the functionality of these receptors in vivo has not been explored in depth. Using a spleen efferocytosis assay and targeted genetic deletion in mice, we identified a multiprotein complex -composed of the receptor tyrosine kinase AXL, LDL receptorrelated protein-1 (LRP-1), and RAN-binding protein 9 (RANBP9) -that mediates DC efferocytosis and antigen cross-presentation. We found that AXL bound ACs, but required LRP-1 to trigger internalization, in murine CD8α + DCs and human-derived DCs. AXL and LRP-1 did not interact directly, but relied on RANBP9, which bound both AXL and LRP-1, to form the complex. In a coculture model of antigen presentation, the AXL/ LRP-1/RANBP9 complex was used by DCs to cross-present AC-associated antigens to T cells. Furthermore, in a murine model of herpes simplex virus-1 infection, mice lacking DC-specific LRP-1, AXL, or RANBP9 had increased AC accumulation, defective viral antigen-specific CD8 + T cell activation, enhanced viral load, and decreased survival. The discovery of this multiprotein complex that mediates functionally important DC efferocytosis in vivo may have implications for future studies related to host defense and DC-based vaccines.

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The Ran binding protein RanBPM interacts with Axl and Sky receptor tyrosine kinases

Cited by 39 publications

References 38 publications

RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors

RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors

TAM Receptor Tyrosine Kinases: Biologic Functions, Signaling, and Potential Therapeutic Targeting in Human Cancer

An AXL/LRP-1/RANBP9 complex mediates DC efferocytosis and antigen cross-presentation in vivo

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