Calmodulin-like Protein Increases Filopodia-dependent Cell Motility via Up-regulation of Myosin-10

Bennett, Richard D.; Mauer, Amy S.; Strehler, Emanuel E.

doi:10.1074/jbc.m607174200

Cited by 50 publications

(57 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…CLP shares ~85% identity with calmodulin, but exhibits approximately eightfold weaker binding to Ca 2+ (Rogers and Strehler, 2001). CLP binds preferentially to the third IQ motif of Myo10 (Caride et al, 2010), and overexpression of CLP increases Myo10 protein levels by several fold, apparently by stabilizing the Myo10 heavy chain during its translation Bennett et al, 2007;.…”

Section: Myo10 Structure and Biochemical Propertiesmentioning

confidence: 99%

Myosin-X: a MyTH-FERM myosin at the tips of filopodia

Kerber

Cheney

2011

Journal of Cell Science

138

131

View full text Add to dashboard Cite

SummaryMyosin-X (Myo10) is an unconventional myosin with MyTH4-FERM domains that is best known for its striking localization to the tips of filopodia and its ability to induce filopodia. Although the head domain of Myo10 enables it to function as an actin-based motor, its tail contains binding sites for several molecules with central roles in cell biology, including phosphatidylinositol (3,4,5)-trisphosphate, microtubules and integrins. Myo10 also undergoes fascinating long-range movements within filopodia, which appear to represent a newly recognized system of transport. Myo10 is also unusual in that it is a myosin with important roles in the spindle, a microtubulebased structure. Exciting new studies have begun to reveal the structure and single-molecule properties of this intriguing myosin, as well as its mechanisms of regulation and induction of filopodia. At the cellular and organismal level, growing evidence demonstrates that Myo10 has crucial functions in numerous processes ranging from invadopodia formation to cell migration.

show abstract

Section: Myo10 Structure and Biochemical Propertiesmentioning

confidence: 99%

Myosin-X: a MyTH-FERM myosin at the tips of filopodia

Kerber

Cheney

2011

Journal of Cell Science

138

131

View full text Add to dashboard Cite

show abstract

“…The inoculated plates were incubated for 7 days and stained with cell stain solution according to the manufacturer's instruction. The number of colonies was determined using BioImaging systems (UVP, LabworksTM, Ver 4.6) (Bennett et al 2007;Hosoi et al 2006).…”

Section: Soft-agar Colony Forming Assaymentioning

confidence: 99%

Growth Inhibitory Effect of the Ternary Complex Factor Net on Human Pancreatic Carcinoma Cell Lines

Zhu

et al. 2008

Tohoku J. Exp. Med.

View full text Add to dashboard Cite

Pancreatic carcinoma is one of the most aggressive malignancies and carries the most dismal prognoses of all cancers. A better understanding of the genes involving in tumor development may allow us to tackle this rapidly progressive disease. The Net gene belongs to the ternary complex transcription factor (TCF) family and is regulated by the Ras/mitogen-activited protein kinase-signaling pathway. Under basal conditions, Net shows strong represssing function on transcription of proto-oncogene gene c-fos. Moreover, the lower expression of Net has been noted in some carcinoma cells, such as cervical cancer. To study the effect of Net on c-fos expression and its potential role in the growth of pancreatic carcinoma, we developed a recombinant plasmid, a pEGFP-N1-Net, which codes for Net-EGFP fusion proteins, and stably transfected it into BxPC-3 human pancreatic carcinoma cells. Using stable transformants, we were able to show that overexpression of Net decreased the expression of c-fos and inhibited pancreatic cancer cell proliferation. Cell cycle analysis demonstrated that Net overexpression inhibited cell cycle progression. These findings suggested that loss of Net repression could augment c-fos expression and further trigger neoplastic cell proliferation, which was involved in the pathogenesis of pancreatic cancer. Therefore, Net might be a potential target for the treatment of c-fos-positive pancreatic cancer.

show abstract

“…CLP competes effectively with calmodulin for Myo10 binding [36] , and upregulation of CLP results in in- Strehler EE. Strehler's profile creased Myo10 expression and function [37] . CLP promotes Myo10 function in filopodial extension and cell migration, and thereby promotes epidermal wound healing [38] .…”

Section: Identification Of Human Calmodulin-like Protein (Calml3) As mentioning

confidence: 99%

Emanuel Strehler’s work on calcium pumps and calcium signaling

Strehler¹

2011

WJBC

View full text Add to dashboard Cite

Cells are equipped with mechanisms to control tightly the influx, efflux and resting level of free calcium (Ca 2+ ). Inappropriate Ca 2+ signaling and abnormal Ca 2+ levels are involved in many clinical disorders including heart disease, Alzheimer's disease and stroke. Ca 2+ also plays a major role in cell growth, differentiation and motility; disturbances in these processes underlie cell transformation and the progression of cancer. Accordingly, research in the Strehler laboratory is focused on a better understanding of the molecular "toolkit" needed to ensure proper Ca 2+ homeostasis in the cell, as well as on the mechanisms of localized Ca 2+ signaling. A longterm focus has been on the plasma membrane calcium pumps (PMCAs), which are linked to multiple disorders including hearing loss, neurodegeneration, and heart disease. Our work over the past 20 years or more has revealed a surprising complexity of PMCA isoforms with different functional characteristics, regulation, and cellular localization. Emerging evidence shows how specific PMCAs contribute not only to setting basal intracellular Ca 2+ levels, but also to local Ca 2+ signaling and vectorial Ca 2+ transport. A second major research area revolves around the calcium sensor protein calmodulin and an enigmatic calmodulin-like protein (CALML3) that is linked to epithelial differentiation. One of the cellular targets of CALML3 is the unconventional motor protein myosin-10, which raises new questions about the role of CALML3 and myosin-10 in cell adhesion and migration in normal cell differentiation and cancer.

show abstract

Calmodulin-like Protein Increases Filopodia-dependent Cell Motility via Up-regulation of Myosin-10

Cited by 50 publications

References 20 publications

Myosin-X: a MyTH-FERM myosin at the tips of filopodia

Myosin-X: a MyTH-FERM myosin at the tips of filopodia

Growth Inhibitory Effect of the Ternary Complex Factor Net on Human Pancreatic Carcinoma Cell Lines

Emanuel Strehler’s work on calcium pumps and calcium signaling

Contact Info

Product

Resources

About