Mammalian CAP (Cyclase-associated protein) in the world of cell migration

Zhou, Guowei; Zhang, Haitao; Field, Jeffrey

doi:10.4161/cam.27479

Cited by 25 publications

(27 citation statements)

References 40 publications

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“…Indeed, it is involved in the turnover of the actin branches, so promoting actin filaments treadmilling and participating to the formation of cell protrusions related to the motile phenotype [131]. This attitude has been proven to be enhanced in malignant cancer cells [132,133]. As already reported, in our tissue we have found four COF1 isoforms, on of which ubiquitous and three sporadic.…”

Section: Cofilin1 Cof1 (Cfl1)supporting

confidence: 68%

Retrospective Proteomic Screening of 100 Breast Cancer Tissues

Pucci‐Minafra¹,

Cara²,

Musso³

et al. 2017

Preprint

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Abstract:The present investigation has been conducted on one hundred tissue fragments of breast cancer, collected and immediately cryopreserved following the surgical resection. The fragments were selected from patients with invasive ductal carcinoma of the breast, the most common and potentially aggressive type of mammary cancer, with the objective to increase the knowledge of breast cancer molecular markers, useful for diagnostic and prognostic categorization of patients, in assessing postsurgical therapeutic regimes. The proteomic screening, by 2D-IPG and mass spectrometry, allowed us to identify two main classes of protein clusters: proteins expressed ubiquitously at high levels in all patients, and proteins expressed sporadically among the same patients. Within the group of ubiquitous proteins, glycolytic enzymes and proteins with anti-apoptotic activity were predominant. Among the sporadic ones, proteins involved in cell motility, molecular chaperones and proteins involved in the detoxification appeared prevalent. The data of the present study indicates that the primary tumor growth is generally supported by two concurrent pathways: the inhibition of apoptosis and the stimulation of cellular proliferation. The second phase of the evolution of the tumor can be prematurely scheduled by the occasional presence of proteins involved in cell motility and in the defenses of the oxidative stress. To our knowledge this report on large-scales proteomics of breast cancer is currently a unique approach in the literature that offers the opportunity to evaluate the presence and recurrence of proteins to be used as prognostic indicators and susceptibility to metastasis in patients operated on for invasive ductal carcinoma of the breast.

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Section: Cofilin1 Cof1 (Cfl1)supporting

confidence: 68%

Retrospective Proteomic Screening of 100 Breast Cancer Tissues

Pucci‐Minafra¹,

Cara²,

Musso³

et al. 2017

Preprint

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“…CAP1 and CAP2 are the two mammalian CAP isoforms. Of the two, CAP1 has been studied more extensively and its function as a regulator of the actin cytoskeleton and cell migration has been solidly established Moriyama and Yahara, 2002;Zhang et al, 2013;Zhou et al, 2014). Our work here focuses on CAP1.…”

Section: Introductionmentioning

confidence: 99%

“…CAPs regulate actin dynamics at multiple levels. They bind and sequester actin monomers to prevent them from polymerizing Gieselmann and Mann, 1992;Zelicof et al, 1996), which helps to maintain a sufficiently large and readily accessible G-actin pool that is essential for rapid actin cytoskeletal reorganization (Zhou et al, 2014). Studies over the past decade have revealed that several domains within CAPs bind to actin, and that CAPs also facilitate nucleotide exchange of ATP onto monomers (Hubberstey and Mottillo, 2002;Ono, 2013).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of the cytoskeletal protein CAP1 controls its association with cofilin and actin

Zhou

Zhang

et al. 2014

Journal of Cell Science

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Cell signaling can control the dynamic balance between filamentous and monomeric actin by modulating actin regulatory proteins. One family of actin regulating proteins that controls actin dynamics comprises cyclase-associated proteins 1 and 2 (CAP1 and 2, respectively). However, cell signals that regulate CAPs remained unknown. We mapped phosphorylation sites on mouse CAP1 and found S307 and S309 to be regulatory sites. We further identified glycogen synthase kinase 3 as a kinase phosphorylating S309. The phosphomimetic mutant S307D/S309D lost binding to its partner cofilin and, when expressed in cells, caused accumulation of actin stress fibers similar to that in cells with reduced CAP expression. In contrast, the non-phosphorylatable S307A/S309A mutant showed drastically increased cofilin binding and reduced binding to actin. These results suggest that the phosphorylation serves to facilitate release of cofilin for a subsequent cycle of actin filament severing. Moreover, our results suggest that S307 and S309 function in tandem; neither the alterations in binding cofilin and/or actin, nor the defects in rescuing the phenotype of the enlarged cell size in CAP1 knockdown cells was observed in point mutants of either S307 or S309. In summary, we identify a novel regulatory mechanism of CAP1 through phosphorylation.

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“…Phosphopeptides from additional 29 phosphoproteins not included in the MRM assays were quantified by SWATH‐MS2. Some interesting examples of phosphopeptides with high biological variation that may be linked to various disease states included IGF‐1, known to be connected with diabetes‐associated cancers , CD44 receptor for extracellular proteins involved in cell migration and tumor growth and progression , vitamin D binding protein (VTDB) known to affect inflammation and cell proliferation in cancer and cardiovascular disease , adenyl cyclase associated protein 1 (CAP1) implicated in cell motility and tumor invasiveness , and SPARK‐like protein 1 (SPRL1) with tumor suppressor function . Interestingly, in addition to the highly variable pS92 on SPRL1, another phosphosite pS295 on SPRL1 had lower biological variability (Supporting Information Table 4).…”

Section: Resultsmentioning

confidence: 99%

Variation and quantification among a target set of phosphopeptides in human plasma by multiple reaction monitoring and SWATH‐MS2 data‐independent acquisition

et al. 2014

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Human plasma contains proteins that reflect overall health and represents a rich source of proteins for identifying and understanding disease pathophysiology. However, few studies have investigated changes in plasma phosphoproteins. In addition, little is known about the normal variations in these phosphoproteins, especially with respect to specific sites of modification. To address these questions, we evaluated variability in plasma protein phosphorylation in healthy individuals using multiple reaction monitoring (MRM) and SWATH MS2 data-independent acquisition. First, we developed a discovery workflow for phosphopeptide enrichment from plasma and identified targets for MRM assays. Next, we analyzed plasma from healthy donors using an analytical workflow consisting of MRM and SWATH MS2 that targeted phosphopeptides from 58 and 68 phosphoproteins, respectively. These two methods produced similar results showing low variability in 13 phosphosites from 10 phosphoproteins (CVinter <30%) and high interpersonal variation of 16 phosphosites from 14 phosphoproteins (CVinter >30%). Moreover, these phosphopeptides originate from phosphoproteins involved in cellular processes governing homeostasis, immune response, cell-extracellular matrix interactions, lipid and sugar metabolism, and cell signaling. This limited assessment of technical and biological variability in phosphopeptides generated from plasma phosphoproteins among healthy volunteers constitutes a reference for future studies that target protein phosphorylation as biomarkers.

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Mammalian CAP (Cyclase-associated protein) in the world of cell migration

Cited by 25 publications

References 40 publications

Retrospective Proteomic Screening of 100 Breast Cancer Tissues

Retrospective Proteomic Screening of 100 Breast Cancer Tissues

Phosphorylation of the cytoskeletal protein CAP1 controls its association with cofilin and actin

Variation and quantification among a target set of phosphopeptides in human plasma by multiple reaction monitoring and SWATH‐MS2 data‐independent acquisition

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