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  1. Article ; Online: Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions.

    Schaller, Michael D

    Journal of cell science

    2010  Volume 123, Issue Pt 7, Page(s) 1007–1013

    Abstract: ... Equally exciting are reports of novel and originally unanticipated functions of these kinases, providing ... important and exciting insights into how FAK and Pyk2 control cellular processes such as cell migration ... Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (Pyk2) are related tyrosine kinases ...

    Abstract Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (Pyk2) are related tyrosine kinases that have important cellular functions, primarily through regulation of the cytoskeleton. Recent studies have identified multiple molecular mechanisms that regulate cytoskeletal responses, and have provided important and exciting insights into how FAK and Pyk2 control cellular processes such as cell migration. Equally exciting are reports of novel and originally unanticipated functions of these kinases, providing the groundwork for future avenues of investigation. This Commentary summarizes some of these recent discoveries that are relevant to the control of biological responses of the cell.
    MeSH term(s) Animals ; Cell Movement ; Cytoskeleton ; Focal Adhesion Kinase 1/metabolism ; GTPase-Activating Proteins/metabolism ; Humans ; Signal Transduction ; rho-Associated Kinases/metabolism
    Chemical Substances GTPase-Activating Proteins ; Focal Adhesion Kinase 1 (EC 2.7.10.2) ; PTK2 protein, human (EC 2.7.10.2) ; rho-Associated Kinases (EC 2.7.11.1) ; ASAP2 protein, human (EC 3.6.1.-)
    Language English
    Publishing date 2010-04-01
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.045112
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: Show issues Location:
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  2. Article: Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions

    Schaller, Michael D

    Journal of cell science. 2010 Apr. 1, v. 123, no. 7

    2010  

    Abstract: ... Equally exciting are reports of novel and originally unanticipated functions of these kinases, providing ... important and exciting insights into how FAK and Pyk2 control cellular processes such as cell migration ... Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (Pyk2) are related tyrosine kinases ...

    Abstract Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (Pyk2) are related tyrosine kinases that have important cellular functions, primarily through regulation of the cytoskeleton. Recent studies have identified multiple molecular mechanisms that regulate cytoskeletal responses, and have provided important and exciting insights into how FAK and Pyk2 control cellular processes such as cell migration. Equally exciting are reports of novel and originally unanticipated functions of these kinases, providing the groundwork for future avenues of investigation. This Commentary summarizes some of these recent discoveries that are relevant to the control of biological responses of the cell.
    Language English
    Dates of publication 2010-0401
    Size p. 1007-1013.
    Publishing place The Company of Biologists Limited
    Document type Article
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Spatial and temporal regulation of focal adhesion kinase activity in living cells.

    Cai, Xinming / Lietha, Daniel / Ceccarelli, Derek F / Karginov, Andrei V / Rajfur, Zenon / Jacobson, Ken / Hahn, Klaus M / Eck, Michael J / Schaller, Michael D

    Molecular and cellular biology

    2007  Volume 28, Issue 1, Page(s) 201–214

    Abstract: ... cells and novel insight into the mechanism regulating FAK conformation. ... for this conformational change and for interaction with a novel ligand for FAK, acidic phospholipids. Binding ... of the kinase was developed. This biosensor was used to probe FAK conformational change in live cells and ...

    Abstract Focal adhesion kinase (FAK) is an essential kinase that regulates developmental processes and functions in the pathology of human disease. An intramolecular autoinhibitory interaction between the FERM and catalytic domains is a major mechanism of regulation. Based upon structural studies, a fluorescence resonance energy transfer (FRET)-based FAK biosensor that discriminates between autoinhibited and active conformations of the kinase was developed. This biosensor was used to probe FAK conformational change in live cells and the mechanism of regulation. The biosensor demonstrates directly that FAK undergoes conformational change in vivo in response to activating stimuli. A conserved FERM domain basic patch is required for this conformational change and for interaction with a novel ligand for FAK, acidic phospholipids. Binding to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing phospholipid vesicles activated and induced conformational change in FAK in vitro, and alteration of PIP2 levels in vivo changed the level of activation of the conformational biosensor. These findings provide direct evidence of conformational regulation of FAK in living cells and novel insight into the mechanism regulating FAK conformation.
    MeSH term(s) Acids ; Amino Acid Motifs ; Amino Acid Sequence ; Biosensing Techniques ; Cell Line ; Cell Survival ; Focal Adhesion Protein-Tyrosine Kinases/chemistry ; Focal Adhesion Protein-Tyrosine Kinases/genetics ; Focal Adhesion Protein-Tyrosine Kinases/metabolism ; Humans ; Models, Molecular ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Phospholipids/metabolism ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary
    Chemical Substances Acids ; Phosphatidylinositol 4,5-Diphosphate ; Phospholipids ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2007-10-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.01324-07
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1666: Show issues Location:
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  4. Article ; Online: Cell surface heat shock protein 90 modulates prostate cancer cell adhesion and invasion through the integrin-β1/focal adhesion kinase/c-Src signaling pathway.

    Liu, Xueguang / Yan, Zuoqin / Huang, Liang / Guo, Muyi / Zhang, Zhigang / Guo, Changan

    Oncology reports

    2011  Volume 25, Issue 5, Page(s) 1343–1351

    Abstract: ... association between FAK, c-Src and integrin β1, but also significantly inhibited the phosphorylation of FAK ... Heat shock protein (Hsp) 90 is a molecular chaperone that maintains the active conformation and ... that molecular targeting of cell surface Hsp90 may therefore be a novel target for the effective treatment ...

    Abstract Heat shock protein (Hsp) 90 is a molecular chaperone that maintains the active conformation and function of numerous client oncoproteins in cancer cells. Hsp90 has also been detected on the plasma membrane of cells, and its expression has been suggested to correlate with metastatic potential. We studied the PC3 cell line, which is a highly invasive human prostate cancer cell line, and confirmed that Hsp90 is present on the cell surface of PC3 cells. Interestingly, cell surface Hsp90 was also specifically localized at the leading edge of migrating cells. By using a specific antibody that inhibited cell surface Hsp90, adhesion and invasion of PC3 cells were significantly suppressed in vitro. Concomitantly with these findings, we demonstrated that the inhibition of cell surface Hsp90 not only inhibited the FN-dependent association between FAK, c-Src and integrin β1, but also significantly inhibited the phosphorylation of FAK and c-Src, as well as their downstream targets paxillin and p130Cas. Additionally, the Hsp90 antibody reversed cell invasion stimulated by overexpression of FAK. These data indicate that cell surface Hsp90 is involved in prostate cancer cell invasion through the integrin β1/FAK/c-Src signaling pathway. Our study provides new insights into the mechanisms of cell surface Hsp90 in cancer invasion. These results suggest that molecular targeting of cell surface Hsp90 may therefore be a novel target for the effective treatment of metastatic prostate cancer.
    MeSH term(s) Antibodies/metabolism ; Antibodies/pharmacology ; Cell Adhesion/drug effects ; Cell Line, Tumor/cytology ; Cell Movement/drug effects ; Fibronectins/metabolism ; Focal Adhesion Protein-Tyrosine Kinases/metabolism ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Integrin beta1/metabolism ; Male ; Prostatic Neoplasms/metabolism ; Prostatic Neoplasms/pathology ; Protein Binding/drug effects ; Protein-Tyrosine Kinases/metabolism ; Signal Transduction/drug effects ; src-Family Kinases
    Chemical Substances Antibodies ; Fibronectins ; HSP90 Heat-Shock Proteins ; Integrin beta1 ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; CSK tyrosine-protein kinase (EC 2.7.10.2) ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2011-05
    Publishing country Greece
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1222484-4
    ISSN 1791-2431 ; 1021-335X
    ISSN (online) 1791-2431
    ISSN 1021-335X
    DOI 10.3892/or.2011.1202
    Database MEDical Literature Analysis and Retrieval System OnLINE

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