Phosphorylation of the Vasodilator-stimulated Phosphoprotein Regulates Its Interaction with Actin

Harbeck, Birgit; Hüttelmaier, Stefan; Schlüter, Kathrin; Jockusch, Brigitte M.; Illenberger, Susanne

doi:10.1074/jbc.m005066200

Cited by 224 publications

(268 citation statements)

References 41 publications

Supporting

Mentioning

250

Contrasting

Unclassified

Order By: Relevance

“…A paradox of these results is that most of the known actin ®lament cross-linking proteins are negatively regulated by PKC phosphorylation which dramatically decreases the abilities of Fascin, MARCKS and VASP to cross-link actin ®laments (Bubb et al, 1999;Harbeck et al, 2000;Hartwig et al, 1992;Huang et al, 1997;Ishikawa et al, 1998;Yamakita et al, 1996). Src phosphorylation similarly inhibits the ability of cortactin to cross-link actin ®laments (Huang et al, 1997).…”

Section: Phosphorylation Of Afap-110 and Its A Ect On Functionmentioning

confidence: 94%

The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity

et al. 2001

View full text Add to dashboard Cite

Section: Phosphorylation Of Afap-110 and Its A Ect On Functionmentioning

confidence: 94%

The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity

et al. 2001

View full text Add to dashboard Cite

“…First, linker-binding energies could be regulated by chemical modification. For example, it has been shown that phosphorylation of the linker protein VASP can affect its binding energy to actin and its bundling activity (30). Alternatively, calcium binding can affect the binding energy of linker proteins to actin (31).…”

Section: Discussionmentioning

confidence: 99%

Structural polymorphism of the cytoskeleton: A model of linker-assisted filament aggregation

Borukhov

Bruinsma

Gelbart

et al. 2005

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

101

View full text Add to dashboard Cite

The phase behavior of charged rods in the presence of interrod linkers is studied theoretically as a model for the equilibrium behavior underlying the organization of actin filaments by linker proteins in the cytoskeleton. The presence of linkers in the solution modifies the effective interrod interaction and can lead to interfilament attraction. Depending on the composition and physical properties of the system, such as linker-binding energies, filaments will orient either perpendicular or parallel to each other, leading to network-like or bundled structures. We show that such a system can have one of three generic phase diagrams, one dominated by bundles, another by networks, and the third containing both bundle and network-like phases. The first two diagrams can be found over a wide range of interaction energies, whereas the third diagram occurs only for a narrow range. These results provide theoretical understanding of the classification of linker proteins as bundling proteins or crosslinking proteins. In addition, they suggest possible mechanisms by which the cell may control cytoskeletal morphology.actin ͉ bundle ͉ liquid crystal ͉ network F ilamentous actin (F-actin) is a highly charged, stiff biopolymer that is abundant in the cell and a key component of the cellular cytoskeleton. A cell controls the assembly of actin filaments into structures ranging from dilute networks, where filaments cross at large angles, to dense bundles, where filaments are closely packed and nearly parallel to one another (1). This structural polymorphism of actin filaments is crucial to cell function because different structures have different roles. Actin bundles have a key role during cell locomotion and cell adhesion (1). However, actin networks near the periphery of an animal cell form the cell cortex, which controls the mechanical properties of the cell surface. To exploit the functional differences between bundles and networks, cells switch between formation of these two structures during cell crawling and cell division (2, 3).Regulation of actin architecture requires control of both the kinetics of assembly and disassembly and of the morphology of actin aggregates. The assembly and disassembly of actin structures are carefully regulated by a number of specific actinbinding proteins, such as branching, capping, and severing proteins (1). However, the morphology, structure, and stability of actin aggregates are controlled by linker proteins, architectural proteins that can bind two filaments together (see refs. 4 and 5 and references therein). These linker proteins are typically classified into bundling proteins, primarily found in bundles, and crosslinking proteins, primarily found in networks. In addition, multivalent cationic species such as Ca 2ϩ , Mg 2ϩ , and spermine can control the morphology of actin aggregation and, therefore, should also be regarded as linkers.In this article, we focus on the equilibrium phase behavior of actin͞linker systems, with a view toward understanding structural polymorphism in the cytosk...

show abstract

“…The phosphorylation of VASP negatively regulates actin nucleation/G-actin binding and interaction with F-actin and some cell adhesion regulators [48][49][50]. On the other hand, VASP binding to focal adhesion protein and profilin, a regulator of actin polymerization, are independent of the VASP phosphorylation status [48,51]. Additionally, the phosphorylation at Ser157 of VASP influenced VASP localization, but little impact on F-actin assembly [14].…”

Section: Udp-induced Vasp Phosphorylation At Ser157 Is Mediated By Rhmentioning

confidence: 99%

Involvement of vasodilator-stimulated phosphoprotein in UDP-induced microglial actin aggregation via PKC- and Rho-dependent pathways

Kataoka¹,

Koga²,

Uesugi³

et al. 2011

Purinergic Signalling

View full text Add to dashboard Cite

Microglia are major immunocompetent cells in the central nervous system and retain highly dynamic motility. The processes which allow these cells to move, such as chemotaxis and phagocytosis, are considered part of their functions and are closely related to purinergic signaling. Previously, we reported that the activation of the P2Y 6 receptor by UDP stimulation in microglia evoked dynamic cell motility which enhanced their phagocytic capacity, as reported by Koizumi et al. (Nature 446 (7139):1091-1095. These responses require actin cytoskeletal rearrangement, which is seen after UDP stimulation. However, the intracellular signaling pathway has not been defined. In this study, we found that UDP in rat primary microglia rapidly induced the transient phosphorylation at Ser157 of vasodilator-stimulated phosphoprotein (VASP). VASP, one of actin binding protein, accumulated at the plasma membrane where filamentous (F)-actin aggregated in a time-dependent manner. The phosphorylation of VASP was suppressed by inhibition of PKC. UDP-induced local actin aggregations were also abrogated by PKC inhibitors. The Rho inhibitor CT04 and the expression of p115-RGS, which suppresses G 12/13 signaling, attenuated UDP-induced phosphorylation of VASP and actin aggregation. These results indicate that PKC-and Rho-dependent phosphorylation of VASP is involved in UDP-induced actin aggregation of microglia.

show abstract

Phosphorylation of the Vasodilator-stimulated Phosphoprotein Regulates Its Interaction with Actin

Cited by 224 publications

References 41 publications

The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity

The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity

Structural polymorphism of the cytoskeleton: A model of linker-assisted filament aggregation

Involvement of vasodilator-stimulated phosphoprotein in UDP-induced microglial actin aggregation via PKC- and Rho-dependent pathways

Contact Info

Product

Resources

About