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Creator | Title | Description | Subject | Date |
1 |
 | Beckerle, Mary C. | Biochemical and molecular characterization of the chicken cysteine-rich protein, a developmentally regulated LIM-domain protein that is associated with the actin cytoskeleton | LIM domains are present in a number of proteins including transcription factors, a protooncogene product, and the adhesion plaque protein zyxin. The LIM domain exhibits a characteristic arrangement of cysteine and histidine residues and represents a novel zinc binding sequence (Michelsen et al., ... | Zyxin; Cysteine-rich proteins; cCRP; Actin; LIM domains | 1994 |
2 |
 | Beckerle, Mary C. | Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression | Members of the cysteine-rich protein (CRP) family are evolutionarily conserved proteins that have been implicated in the processes of cell proliferation and differentiation. In particular, one CRP family member has been shown to be an essential regulator of cardiac and skeletal muscle development. | LIM domains; Chicken fibroblasts; Zyxin; Actinin; Protein expression; Cysteine-rich proteins | 1997 |
3 |
 | Beckerle, Mary C.; Clark, Kathleen A. | Conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans | We describe here the molecular and functional characterization of the Caenorhabditis elegans unc-97 gene, whose gene product constitutes a novel component of muscular adherens junctions. UNC-97 and homologues from several other species define the PINCH family, a family of LIM proteins whose modula... | LIM domains; Caenorhabditis elegans; UNC-97; Adherens junction; Touch neuron; Muscle development | 1999 |
4 |
 | Beckerle, Mary C. | CRP1, a LIM domain protein implicated in muscle differentiation, interacts with α-actinin | Members of the cysteine-rich protein (CRP) family are LIM domain proteins that have been implicated in muscle differentiation. One strategy for defining the mechanism by which CRPs potentiate myogenesis is to characterize the repertoire of CRP binding partners. | CRP1; Cysteine-rich proteins; Actinin; Protein-protein interactions; LIM domains | 1997 |
5 |
 | Beckerle, Mary C. | Cysteine-rich protein family of highly related LIM domain proteins | Here we describe a family of closely related LIM domain proteins in avian cells. The LIM motif defines a zinc-binding domain that is found in a variety of transcriptional regulators, proto-oncogene products, and proteins associated with sites of cell-substratum contact. One type of LIM-domain protei... | LIM domains; Chicken embryo fibroblasts; Quail embryo fibroblasts; Cell growth; Cell development; Cysteine-rich proteins | 1995 |
6 |
 | Beckerle, Mary C. | LIM domain-containing protein Trip6 can act as a coactivator for the v-Rel transcription factor | The retroviral oncoprotein v-Rel is a transcriptional activator in the Rel/NF-KB family of eukaryotic transcription factors. v-Rel malignantly transforms a variety of cell types in vitro and in vivo, and its transforming activity is dependent on the ability of v-Rel to bind to DNA and activate trans... | LIM domains; Oncoproteins; v-Rel; Retroviral oncogene; Trip6; Coactivator; Malignant transformation; NF-kB; Two-hybrid assay | 1999 |
7 |
 | Beckerle, Mary C. | Members of the zyxin family of LIM proteins interact with members of the p130cas family of signal transducers | Integrin binding to extracellular matrix proteins induces formation of signaling complexes at focal adhesions. Zyxin co-localizes with integrins at sites of cellsubstratum adhesion and is postulated to serve as a docking site for the assembly of multimeric protein complexes involved in regulating ce... | Zyxin; Actin; LIM domains; Trip6; Focal adhesions | 2002 |
8 |
 | Beckerle, Mary C. | Molecular characterization of human zyxin | Zyxin is a component of adhesion plaques that has been suggested to perform regulatory functions at these specialized regions of the plasma membrane. Here we describe the isolation and characterization of cDNAs encoding human and mouse zyxin. | Zyxin; Proline; LIM domains | 1996 |
9 |
 | Beckerle, Mary C. | Molecular dissection of a LIM domain | LIM domains are novel sequence elements that are found in more than 60 gene products, many of which function as key regulators of developmental pathways. The LIM domain, characterized by the cysteine-rich consensus CX2CX16_23HX2CX2CX2CX16_21CX2-3(C/H/ D), is a specific metal-binding structure tha... | LIM domains; Metal-binding; Zyxin; Cysteine-rich proteins | 1997 |
10 |
 | Beckerle, Mary C. | Muscle LIM proteins are associated with muscle sarcomeres and require dMEF2 for their expression during Drosophila myogenesis | A genetic hierarchy of interactions, involving myogenic regulatory factors of the MyoD and myocyte enhancer-binding 2 (MEF2) families, serves to elaborate and maintain the differentiated muscle phenotype through transcriptional regulation of muscle-specific target genes. | LIM domains; Cysteine-rich proteins | 1999 |
11 |
 | Beckerle, Mary C.; Davis, Darrell R.; Winge, Dennis R. | Mutational analysis of the metal sites in an LIM domain | Site-directed mutagenesis was carried out map the residues that form the two Zn(I1) sites within a LIM domain. The C-terminal LIM domain derived from the cysteine-rich protein was utilized for this analysis and is referred to as LIMB. | LIM domains; Metal-binding | 1994 |
12 |
 | Beckerle, Mary C. | Opposing roles of zyxin/LPP ACTA repeats and the LIM domain region in cell-cell adhesion | Cadherins mediate cell-cell adhesion by linking cell junctions to actin networks. Although several actin regulatory systems have been implicated in cell-cell adhesion, it remains unclear how such systems drive cadherin-actin network formation and how they are regulated to coincide with initiation o... | Zyxin; Actin; Cadherin; LIM domains; VASP | 2006 |
13 |
 | Beckerle, Mary C. | Purification and characterization of an α-actinin-binding PDZ-LIM protein that is up-regulated during muscle differentiation | α-Actinin is required for the organization and function of the contractile machinery of muscle. In order to understand more precisely the molecular mechanisms by which α-actinin might contribute to the formation and maintenance of the contractile apparatus within muscle cells, we performed a scree... | LIM domains; Z-disc; Actin; Actinin-associated LIM proteins; PDZ-LIM protein | 1999 |
14 |
 | Beckerle, Mary C.; Hoffman, Laura M. | Supervillin modulation of focal adhesions involving TRIP6/ZRP-1 | Cell-substrate contacts, called focal adhesions (FAs), are dynamic in rapidly moving cells. We show that supervillin (SV)-a peripheral membrane protein that binds myosin II and F-actin in such cells-negatively regulates stress fibers, FAs, and cell-substrate adhesion. The major FA regulatory sequenc... | Supervillin; Focal adhesions; Zyxin; LIM domains; TRIP6 | 2006 |
15 |
 | Beckerle, Mary C. | Targeting of zyxin to sites of actin membrane interaction and to the nucleus | The localization of proteins to particular intracellular compartments often regulates their functions. Zyxin is a LIM protein found prominently at sites of cell adhesion, faintly in leading lamellipodia, and transiently in cell nuclei. Here we have performed a domain analysis to identify regions in ... | Zyxin; Actin; LIM domains; Focal adhesions; Lamellipodia; Cytoskeletal architecture | 2001 |
16 |
 | Beckerle, Mary C. | Two muscle-specific LIM proteins in Drosophila | The LIM domain defines a zinc-binding motif found in a growing number of eukaryotic proteins that regulate cell growth and differentiation during development. Members of the cysteine-rich protein (CRP) family of LIM proteins have been implicated in muscle differentiation in vertebrates. Here we r... | LIM domains; Mlp60A; Mlp84B; Cysteine-rich proteins | 1996 |