I-BAR protein antagonism of endocytosis mediates directional sensing during guided cell migration

Quiñones, Gabriel; Jin, Janet; Oro, Anthony E.

doi:10.1083/jcb.200910136

Cited by 57 publications

(65 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Hence, our data together with other studies demonstrate that MIM is implicated in the membrane dynamics of endocytic vesicles. In addition to its association with endosomes, MIM has been also implicated in antagonizing the complex of cortactin and the CD2-associated protein, and in inhibition of the endocytosis of EGF and in directional border cell migration in Drosophila (Quinones et al, 2010). The difference between our observations and that report may reflect the multiple roles of MIM in endocytosis under different contexts, as described in these studies.…”

Section: Discussioncontrasting

confidence: 57%

Missing-in-metastasis protein downregulates CXCR4 by promoting ubiquitylation and interaction with small Rab GTPases

Baxter

et al. 2017

Journal of Cell Science

View full text Add to dashboard Cite

Surface expression of chemokine receptor CXCR4 is downregulated by missing-in-metastasis protein (MIM; also known as MTSS1), a member of the inverse BAR (I-BAR)-domain protein family that recognizes and generates membranes with negative curvature. Yet, the mechanism for the regulation is unknown. Here, we show that MIM forms a complex with CXCR4 by binding to E3 ubiquitin ligase AIP4 (also known as ITCH) in response to stromal cell-derived factor 1 (SDF-1; also known as CXCL12). Overexpression of MIM promoted CXCR4 ubiquitylation, inhibited cellular response to SDF-1, caused accumulation and aggregation of multivesicular bodies (MVBs) in the cytoplasm, and promoted CXCR4 sorting into MVBs in a manner depending on binding to AIP4. In response to SDF-1, MIM also bound transiently to the small GTPase Rab5 at 5 min and to Rab7 at 30 min. Binding to Rab7 requires an N-terminal coiled-coil motif, deletion of which abolished MIM-mediated MVB formation and CXCR4 internalization. Our results unveil a previously unknown property of MIM that establishes the linkage of protein ubiquitylation with Rab-guided trafficking of CXCR4 in endocytic vesicles.

show abstract

Section: Discussioncontrasting

confidence: 57%

Missing-in-metastasis protein downregulates CXCR4 by promoting ubiquitylation and interaction with small Rab GTPases

Baxter

et al. 2017

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…CINDR has three SH3 domains and positively regulates receptor-mediated endocytosis (29). Kometani et al (30) demonstrated that CIN85 functions upstream of IKKβ in the activation of NF-κB in B cells and is responsible for T-cell-independent type II antibody responses in vivo.…”

Section: Discussionmentioning

confidence: 99%

Landscape of protein–protein interactions in Drosophila immune deficiency signaling during bacterial challenge

Fukuyama

Verdier

Guan

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The Drosophila defense against pathogens largely relies on the activation of two signaling pathways: immune deficiency (IMD) and Toll. The IMD pathway is triggered mainly by Gram-negative bacteria, whereas the Toll pathway responds predominantly to Gram-positive bacteria and fungi. The activation of these pathways leads to the rapid induction of numerous NF-κB–induced immune response genes, including antimicrobial peptide genes. The IMD pathway shows significant similarities with the TNF receptor pathway. Recent evidence indicates that the IMD pathway is also activated in response to various noninfectious stimuli (i.e., inflammatory-like reactions). To gain a better understanding of the molecular machinery underlying the pleiotropic functions of this pathway, we first performed a comprehensive proteomics analysis to identify the proteins interacting with the 11 canonical members of the pathway initially identified by genetic studies. We identified 369 interacting proteins (corresponding to 291 genes) in heat-killed Escherichia coli- stimulated Drosophila S2 cells, 92% of which have human orthologs. A comparative analysis of gene ontology from fly or human gene annotation databases points to four significant common categories: ( i ) the NuA4, nucleosome acetyltransferase of H4, histone acetyltransferase complex, ( ii ) the switching defective/sucrose nonfermenting-type chromatin remodeling complex, ( iii ) transcription coactivator activity, and ( iv ) translation factor activity. Here we demonstrate that sumoylation of the IκB kinase homolog immune response-deficient 5 plays an important role in the induction of antimicrobial peptide genes through a highly conserved sumoylation consensus site during bacterial challenge. Taken together, the proteomics data presented here provide a unique avenue for a comparative functional analysis of proteins involved in innate immune reactions in flies and mammals.

show abstract

“…More recently, a Drosophila I-BAR domain protein that is related to mouse MIM and ABBA was shown to interact with this actin-binding protein to promote directional cell migration (Lin et al, 2005;Quinones et al, 2010). We thus generated a MIM construct where the previously identified cortactin-binding site was deleted (Lin et al, 2005).…”

Section: Mim Promotes Actin and Membrane Dynamics At Adherens Junctiomentioning

confidence: 99%

Missing-in-metastasis MIM/MTSS1 promotes actin assembly at intercellular junctions and is required for integrity of kidney epithelia

Saarikangas

Mattila

Varjosalo

et al. 2011

Journal of Cell Science

View full text Add to dashboard Cite

SummaryMIM/MTSS1 is a tissue-specific regulator of plasma membrane dynamics, whose altered expression levels have been linked to cancer metastasis. MIM deforms phosphoinositide-rich membranes through its I-BAR domain and interacts with actin monomers through its WH2 domain. Recent work proposed that MIM also potentiates Sonic hedgehog (Shh)-induced gene expression. Here, we generated MIM mutant mice and found that full-length MIM protein is dispensable for embryonic development. However, MIM-deficient mice displayed a severe urinary concentration defect caused by compromised integrity of kidney epithelia intercellular junctions, which led to bone abnormalities and end-stage renal failure. In cultured kidney epithelial (MDCK) cells, MIM displayed dynamic localization to adherens junctions, where it promoted Arp2/3-mediated actin filament assembly. This activity was dependent on the ability of MIM to interact with both membranes and actin monomers. Furthermore, results from the mouse model and cell culture experiments suggest that full-length MIM is not crucial for Shh signaling, at least during embryogenesis. Collectively, these data demonstrate that MIM modulates interplay between the actin cytoskeleton and plasma membrane to promote the maintenance of intercellular contacts in kidney epithelia.

show abstract

I-BAR protein antagonism of endocytosis mediates directional sensing during guided cell migration

Cited by 57 publications

References 61 publications

Missing-in-metastasis protein downregulates CXCR4 by promoting ubiquitylation and interaction with small Rab GTPases

Missing-in-metastasis protein downregulates CXCR4 by promoting ubiquitylation and interaction with small Rab GTPases

Landscape of protein–protein interactions in Drosophila immune deficiency signaling during bacterial challenge

Missing-in-metastasis MIM/MTSS1 promotes actin assembly at intercellular junctions and is required for integrity of kidney epithelia

Contact Info

Product

Resources

About