Phosphorylation of theDictyostelium myosin II heavy chain is necessary for maintaining cellular polarity and suppressing turning during chemotaxis

Stites, Janice; Wessels, Deborah; Uhl, Amanda M.; Egelhoff, Thomas; Shutt, Damon C.; Soll, David R.

doi:10.1002/(sici)1097-0169(1998)39:1<31::aid-cm4>3.0.co;2-j

Cited by 76 publications

(47 citation statements)

References 50 publications

(120 reference statements)

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“…The roundness of these cells was calculated by using the Eq. 100 ϫ 4 (area/perimeter 2 ) (55). This equation provides a measurement of how efficiently a given amount of perimeter encloses an area: a circle has the largest area for any given perimeter with a roundness of 100%.…”

Section: Methodsmentioning

confidence: 99%

Bves directly interacts with GEFT, and controls cell shape and movement through regulation of Rac1/Cdc42 activity

Smith

Hager

Francis

et al. 2008

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

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Bves is an integral membrane protein with no determined function and no homology to proteins outside of the Popdc family. It is widely expressed throughout development in myriad organisms. Here, we demonstrate an interaction between Bves and guanine nucleotide exchange factor T (GEFT), a GEF for Rho-family GTPases. This interaction represents the first identification of any protein that has a direct physical interaction with any member of the Popdc family. Bves and GEFT are shown to colocalize in adult skeletal muscle. We also demonstrate that exogenous expression of Bves reduces Rac1 and Cdc42 activity levels while not affecting levels of active RhoA. Consistent with a repression of Rac1 and Cdc42 activity, we show changes in speed of cell locomotion and cell roundness also result from exogenous expression of Bves. Modulation of Rho-family GTPase signaling by Bves would be highly consistent with previously described phenotypes occurring upon disruption of Bves function in a wide variety of model systems. Therefore, we propose Bves as a novel regulator of the Rac1 and Cdc42 signaling cascades.Popdc ͉ cell motility ͉ GEF

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Section: Methodsmentioning

confidence: 99%

Bves directly interacts with GEFT, and controls cell shape and movement through regulation of Rac1/Cdc42 activity

Smith

Hager

Francis

et al. 2008

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

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“…4B). RhoA effects on neutrophil chemotaxis are mediated in part via induction of ROCK, a RhoA-binding kinase that promotes MLC activation via its serine phosphorylation and posterior translocation in the cell (27,28). As shown in Fig.…”

Section: Mdia1 Promotes Larg Induction Of Rhoa-rock Signalingmentioning

confidence: 99%

The mDial Formin Is Required for Neutrophil Polarization, Migration, and Activation of the LARG/RhoA/ROCK Signaling Axis during Chemotaxis

Shi

Zhang

Mullin

et al. 2009

The Journal of Immunology

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Neutrophil chemotaxis depends on actin dynamics, but the roles for specific cytoskeleton regulators in this response remain unclear. By analysis of mammalian diaphanous-related formin 1 (mDia1)-deficient mice, we have identified an essential role for this actin nucleator in neutrophil chemotaxis. Lack of mDia1 was associated with defects in chemoattractant-induced neutrophil actin polymerization, polarization, and directional migration, and also with impaired activation of RhoA, its downstream target p160-Rho-associated coil-containing protein kinase (ROCK), and the leukemia-associated RhoA guanine nucleotide exchange factor (LARG). Our data also revealed mDia1 to be associated with another cytoskeletal regulator, Wiskott-Aldrich syndrome protein (WASp), at the leading edge of chemotaxing neutrophils and revealed polarized morphology and chemotaxis to be more mildly impaired in WAS ؊/؊ than in mDia1 ؊/؊ neutrophils, but essentially abrogated by combined mDia1/WASp deficiency. Thus, mDia1 roles in neutrophil chemotaxis appear to be subserved in concert with WASp and are realized at least in part by activation of the LARG/RhoA/ROCK signaling pathway.

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“…However, Wessels et al found that pten -cells are defective in myosin II assembly at the cell cortex in response to chemoattractant, providing insight into the possible mechanism underlying the lack of repression of lateral pseudopodia in these cells (Wessels et al, 2007). Indeed, myosin II normally localizes to the sides and rear of chemotactic neutrophils and Dictyostelium cells, where it prevents the formation of lateral pseudopodia and promotes cell body contraction and posterior retraction (Heid et al, 2005;Heid et al, 2004;Stites et al, 1998;Uchida et al, 2003;Wessels et al, 1988;Xu et al, 2003). Given its sequence similarity to the actin-binding protein tensin, Wessels et al further suggest that PTEN could directly interact with and modulate the F-actin-myosin cytoskeleton, implying that PTEN could play a role in cytoskeleton regulation that is independent of its PtdIns(3,4,5)P 3 phosphatase activity.…”

Section: Chemotaxis In the Absence Of Pi3k And/or Ptenmentioning

confidence: 99%

The regulation of cell motility and chemotaxis by phospholipid signaling

Kölsch

Charest

Firtel

2008

Journal of Cell Science

317

315

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Phosphoinositide 3-kinase (PI3K), PTEN and localized phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P 3 ] play key roles in chemotaxis, regulating cell motility by controlling the actin cytoskeleton in Dictyostelium and mammalian cells. PtdIns(3,4,5)P 3 , produced by PI3K, acts via diverse downstream signaling components, including the GTPase Rac, Arf-GTPases and the kinase Akt (PKB). It has become increasingly apparent, however, that chemotaxis results from an interplay between the PI3K-PTEN pathway and other parallel pathways in Dictyostelium and mammalian cells. In Dictyostelium, the phospholipase PLA2 acts in concert with PI3K to regulate chemotaxis, whereas phospholipase C (PLC) plays a supporting role in modulating PI3K activity. In adenocarcinoma cells, PLC and the actin regulator cofilin seem to provide the direction-sensing machinery, whereas PI3K might regulate motility.

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Phosphorylation of theDictyostelium myosin II heavy chain is necessary for maintaining cellular polarity and suppressing turning during chemotaxis

Cited by 76 publications

References 50 publications

Bves directly interacts with GEFT, and controls cell shape and movement through regulation of Rac1/Cdc42 activity

Bves directly interacts with GEFT, and controls cell shape and movement through regulation of Rac1/Cdc42 activity

The mDial Formin Is Required for Neutrophil Polarization, Migration, and Activation of the LARG/RhoA/ROCK Signaling Axis during Chemotaxis

The regulation of cell motility and chemotaxis by phospholipid signaling

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