An extracellular matrix, calmodulin-binding protein from Dictyostelium with EGF-like repeats that enhance cell motility

Suarez, Andres; Huber, Robert J.; Myre, Michael A.; O’Day, Danton H.

doi:10.1016/j.cellsig.2011.03.008

Cited by 18 publications

(59 citation statements)

References 52 publications

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“…A cdk5-GFP expression vector was generated according to previously described procedures (Suarez et al 2011). cDNA was amplified by PCR using the PfuUltra II Fusion HS DNA Polymerase master mix (Agilent Technologies Canada Inc., Mississauga, ON, Canada) and the following forward and reverse primers, respectively; 5 0 -CAAGAT CTAAAATGGAGAAATATTCAAAAATTG-3 0 and 5 0 -CA ACTAGTATTAATAGGTTCTAAACCATC-3 0 .…”

Section: Construction Of a Cdk5-gfp Expression Vectormentioning

confidence: 99%

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Nucleocytoplasmic transfer of cyclin dependent kinase 5 and its binding to puromycin-sensitive aminopeptidase in Dictyostelium discoideum

Huber

O’Day

2011

Histochem Cell Biol

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The Dictyostelium discoideum homolog of mammalian cyclin dependent kinase 5 (Cdk5) has previously been shown to be required for optimal growth and differentiation in this model organism, however, the subcellular localization of the protein has not previously been studied. In this study, immunolocalizations and a GFP fusion construct localized Cdk5 predominantly to the nucleus of vegetative cells. Western blots showed that Cdk5 was present in both nuclear and non-nuclear fractions, suggesting a functional role in both cellular locales. During the early stages of mitosis, Cdk5 gradually moved from a punctate nucleoplasmic distribution to localize adjacent to the inner nuclear envelope. During anaphase and telophase, Cdk5 localized to the cytoplasm and was not detected in the nucleoplasm. Cdk5 returned to the nucleus during cytokinesis. Proteolytic activity has been shown to be a critical regulator of the cell cycle. Immunoprecipitations coupled with immunolocalizations identified puromycin-sensitive aminopeptidase A (PsaA) as a potential Cdk5 binding partner in Dictyostelium. Immunoprecipitations also identified two phosphotyrosine proteins (35 and 18 kDa) that may interact with Cdk5 in vivo. Together, this work provides new insight into the localization of Cdk5, its function during cell division, and its binding to a proteolytic enzyme in Dictyostelium.

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Section: Construction Of a Cdk5-gfp Expression Vectormentioning

confidence: 99%

“…The plasmid carrying the correct in-frame insertion was named pDM323-cdk5GFP. AX3 cells were transformed by electroporation with pDM323-cdk5GFP according to previously established procedures Suarez et al 2011). The resulting strain was named AX3/[act15]:cdk5:GFP.…”

Section: Construction Of a Cdk5-gfp Expression Vectormentioning

confidence: 99%

Nucleocytoplasmic transfer of cyclin dependent kinase 5 and its binding to puromycin-sensitive aminopeptidase in Dictyostelium discoideum

Huber

O’Day

2011

Histochem Cell Biol

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“…CyrA is the first extracellular matrix (ECM; slime sheath), calmodulin (CaM)-binding protein (CaMBP) identified in the model eukaryote Dictyostelium discoideum (Suarez et al, 2011). This 63 kDa cysteine-rich protein is proteolytically cleaved during asexual development to release two prominent epidermal growth factor-like (EGFL) repeat-containing cleavage products of molecular weights 45 and 40 kDa (named CyrA-C45 and CyrA-C40, respectively) (Suarez et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…This 63 kDa cysteine-rich protein is proteolytically cleaved during asexual development to release two prominent epidermal growth factor-like (EGFL) repeat-containing cleavage products of molecular weights 45 and 40 kDa (named CyrA-C45 and CyrA-C40, respectively) (Suarez et al, 2011). EGFL repeat-containing proteins are often found to be membrane-bound or secreted components of the ECM (Campbell and Bork, 1993).…”

Section: Introductionmentioning

confidence: 99%

CyrA, a matricellular protein that modulates cell motility in Dictyostelium discoideum

2012

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“…Scale bars: 1 m. controlling gene expression and cell motility (Kolbinger et al, 2005;Yamada et al, 2010;Suarez et al, 2011). Evidently, CTDC domaincontaining genes were strongly amplified in early Dictyostelid evolution, and from this pool of matrix components, genes with novel signalling roles emerged.…”

Section: Improvement Of Camp Signalling Dynamics By Recruitment Of a mentioning

confidence: 99%

Evolution of self-organisation in Dictyostelia by adaptation of a non-selective phosphodiesterase and a matrix component for regulated cAMP degradation

et al. 2012

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SUMMARYDictyostelium discoideum amoebas coordinate aggregation and morphogenesis by secreting cyclic adenosine monophosphate (cAMP) pulses that propagate as waves through fields of cells and multicellular structures. To retrace how this mechanism for selforganisation evolved, we studied the origin of the cAMP phosphodiesterase PdsA and its inhibitor PdiA, which are essential for cAMP wave propagation. D. discoideum and other species that use cAMP to aggregate reside in group 4 of the four major groups of Dictyostelia. We found that groups 1-3 express a non-specific, low affinity orthologue of PdsA, which gained cAMP selectivity and increased 200-fold in affinity in group 4. A low affinity group 3 PdsA only partially restored aggregation of a D. discoideum pdsA-null mutant, but was more effective at restoring fruiting body morphogenesis. Deletion of a group 2 PdsA gene resulted in disruption of fruiting body morphogenesis, but left aggregation unaffected. Together, these results show that groups 1-3 use a low affinity PdsA for morphogenesis that is neither suited nor required for aggregation. PdiA belongs to a family of matrix proteins that are present in all Dictyostelia and consist mainly of cysteine-rich repeats. However, in its current form with several extensively modified repeats, PdiA is only present in group 4. PdiA is essential for initiating spiral cAMP waves, which, by organising large territories, generate the large fruiting structures that characterise group 4. We conclude that efficient cAMPmediated aggregation in group 4 evolved by recruitment and adaptation of a non-selective phosphodiesterase and a matrix component into a system for regulated cAMP degradation.

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An extracellular matrix, calmodulin-binding protein from Dictyostelium with EGF-like repeats that enhance cell motility

Cited by 18 publications

References 52 publications

Nucleocytoplasmic transfer of cyclin dependent kinase 5 and its binding to puromycin-sensitive aminopeptidase in Dictyostelium discoideum

Nucleocytoplasmic transfer of cyclin dependent kinase 5 and its binding to puromycin-sensitive aminopeptidase in Dictyostelium discoideum

CyrA, a matricellular protein that modulates cell motility in Dictyostelium discoideum

Evolution of self-organisation in Dictyostelia by adaptation of a non-selective phosphodiesterase and a matrix component for regulated cAMP degradation

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