Identification of a novel protein complex containing annexin VI, Fyn, Pyk2, and the p120GAP C2 domain

@article{Chow2000IdentificationOA,
  title={Identification of a novel protein complex containing annexin VI, Fyn, Pyk2, and the p120GAP C2 domain},
  author={Angela Chow and Alison J. Davis and Debra J. Gawler},
  journal={FEBS Letters},
  year={2000},
  volume={469}
}

Molecular mechanisms involved in Ras inactivation: the annexin A6–p120GAP complex

  • T. GrewalC. Enrich
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 2006
How annexin A6 modulates the involvement of negative regulators of the Ras–Raf–MAPK pathway contributing to Ras inactivation is discussed, including the translocation and complex formation of GTPase‐activating proteins at the plasma membrane to inactivate Ras.

Annexin A6—A multifunctional scaffold in cell motility

This review will discuss how the multiple scaffold functions may enable AnxA6 to modulate migratory cell behavior in health and disease.

Annexins: from structure to function.

Although annexins lack signal sequences for secretion, some members of the family have also been identified extracellularly where they can act as receptors for serum proteases on the endothelium as well as inhibitors of neutrophil migration and blood coagulation.

Annexin A6 is an organizer of membrane microdomains to regulate receptor localization and signalling

The regulation of cell surface receptors by AnxA6 may be facilitated by its unique structure that allows recruitment of interaction partners and simultaneously bridging specialized membrane domains with cortical actin surrounding activated receptors.

Annexin A6-Linking Ca(2+) signaling with cholesterol transport.

Identification of a novel interaction between the Ca(2+)-binding protein S100A11 and the Ca(2+)- and phospholipid-binding protein annexin A6.

It is hypothesized that an agonist-induced increase in cytosolic free [Ca(2+)] leads to formation of a complex of S100A11 and annexin A6, which forms a physical connection between the plasma membrane and the cytoskeleton, or plays a role in the formation of signaling complexes at the level of the sarcolemma.

Role of annexin A 6 in cancer ( Review )

In several types of cancer, AnxA6 acts via Ras, Ras/MAPK and/or FAK/PI3K signaling pathways by mainly mediating PKCα, p120GAP, Bcr-Abl and YY1.

Role of annexin A6 in cancer (Review)

In several types of cancer, AnxA6 acts via Ras, Ras/MAPK and/or FAK/PI3K signaling pathways by mainly mediating PKCα, p120GAP, Bcr-Abl and YY1.

GTP-binding properties of the membrane-bound form of porcine liver annexin VI.

It is suggested that AnxVI is a GTP-binding protein and the binding of the nucleotide may have a regulatory impact on the interaction of annexin with membranes, e.g. formation of ion channels by the protein.

References

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The Ca2+-dependent lipid binding domain of P120GAP mediates protein-protein interactions with Ca2+-dependent membrane-binding proteins. Evidence for a direct interaction between annexin VI and P120GAP.

The CaLB domain in P120(GAP) appears to have the ability to direct specific protein-protein interactions with Ca2+-dependent membrane-associated proteins.

Potential interaction between annexin VI and a 56-kDa protein kinase in T cells.

Annexins belong to a large family of calcium-dependent phospholipid binding proteins known to undergo post-translational modifications such as phosphorylation, and among annexins found in Jurkat cells, annexin VI was shown to be phosphorylated in vitro by p56lck and annexins I and II by p60src.

Mutation-deletion analysis of a Ca(2+)-dependent phospholipid binding (CaLB) domain within p120 GAP, a GTPase-activating protein for p21 ras.

It is established that amino acids 612-643 of p120 GAP indeed constitute a functional CaLB domain and thereby imply a role for Ca2+ in the regulation of p 120 GAP association with cellular (membrane) phospholipids.

The C2 domain calcium‐binding motif: Structural and functional diversity

The present review summarizes the information currently available regarding the structure and function of the C2 domain and provides a novel sequence alignment of 65 C2domain primary structures that predicts that C2 domains form two distinct topological folds.

Cloning of bovine GAP and its interaction with oncogenic ras p21

It is shown that GAP interacts preferentially with the active GTP complexes of both normal and oncogenic Harvey (Ha) ras p21 compared with the inactive GDP complexes.

Induction of Apoptosis after Expression of PYK2, a Tyrosine Kinase Structurally Related to Focal Adhesion Kinase

The results suggest that PYK2 and FAK, albeit highly homologous in primary structure, appear to have different functions; FAK is required for cell survival, whereas PyK2 induces apoptosis in fibroblasts.

T cell receptor engagement induces tyrosine phosphorylation of FAK and Pyk2 and their association with Lck.

FAK and Pyk2 are two of the major 115-to-120-kDa proteins that become tyrosine phosphorylated in T cells following TCR complex stimulation and an association of these kinases with the SH2 domain of the tyrosin kinase Lck in vivo is shown in vivo.

A novel mammalian Ras GTPase-activating protein which has phospholipid-binding and Btk homology regions

Results clearly show that Gap1m, a mammalian counterpart of the Drosophila Gap1 gene, is a novel Ras GAP molecule of mammalian cells.

Interaction of both the C2A and C2B domains of rabphilin3 with Ca2+ and phospholipid.

Rabphilin3 interacts with Ca2+ and phospholipid at its C2 domain, but it remains to be clarified which domain, the C2A or C2B domain, interacts with these compounds.