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1.
Cell Biol Educ ; 2(1): 35-50, 2003.
Article in English | MEDLINE | ID: mdl-12822037

ABSTRACT

Multimedia has the potential of providing bioscience education novel learning environments and pedagogy applications to foster student interest, involve students in the research process, advance critical thinking/problem-solving skills, and develop conceptual understanding of biological topics. Cancer Cell Biology, an interactive, multimedia, problem-based module, focuses on how mutations in protooncogenes and tumor suppressor genes can lead to uncontrolled cell proliferation by engaging students as research scientists/physicians with the task of diagnosing the molecular basis of tumor growth for a group of patients. The process of constructing the module, which was guided by scientist and student feedback/responses, is described. The completed module and insights gained from its development are presented as a potential "multimedia pedagogy" for the development of other multimedia science learning environments.


Subject(s)
Biology/education , Cells , Multimedia , Neoplasms/pathology , Computer-Assisted Instruction , Educational Technology/methods , Humans , Problem Solving , Problem-Based Learning/methods , Science/education , Software Design , Students , Thinking
2.
J Biol Chem ; 277(11): 9580-9, 2002 Mar 15.
Article in English | MEDLINE | ID: mdl-11782456

ABSTRACT

Integrin binding to extracellular matrix proteins induces formation of signaling complexes at focal adhesions. Zyxin co-localizes with integrins at sites of cell-substratum adhesion and is postulated to serve as a docking site for the assembly of multimeric protein complexes involved in regulating cell motility. Recently, we identified a new member of the zyxin family called TRIP6. TRIP6 is localized at focal adhesions and overexpression of TRIP6 slows cell migration. In an effort to define the molecular mechanism by which TRIP6 affects cell migration, the yeast two-hybrid assay was employed to identify proteins that directly bind to TRIP6. This assay revealed that both TRIP6 and zyxin interact with CasL/HEF1, a member of the Cas family. This association is mediated by the LIM region of the zyxin family members and the SH2 domain-binding region of CasL/HEF1. Furthermore, the association between p130(Cas) and the two zyxin family members was demonstrated to occur in vivo by co-immunoprecipitation. Zyxin and Cas family members may cooperate to regulate cell motility.


Subject(s)
Adaptor Proteins, Signal Transducing , Metalloproteins/metabolism , Phosphoproteins/metabolism , Proteins , Transcription Factors/metabolism , ATPases Associated with Diverse Cellular Activities , Amino Acid Sequence , Animals , Cell Adhesion , Cell Movement , Crk-Associated Substrate Protein , LIM Domain Proteins , Molecular Sequence Data , Proteasome Endopeptidase Complex , Rabbits , Retinoblastoma-Like Protein p130 , Two-Hybrid System Techniques
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