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We are analyzing https://www.tandfonline.com/doi/full/10.1128/mcb.20.3.1044-1054.2000.

Title:
Death-Associated Protein Kinase-Related Protein 1, a Novel Serine/Threonine Kinase Involved in Apoptosis: Molecular and Cellular Biology: Vol 20 , No 3 - Get Access
Description:
Apoptosis is a genetically controlled cell death process which is important at various developmental stages as well as for cell maintenance and tissue homeostasis (16). During the last few years, m...
Website Age:
19 years and 10 months (reg. 2005-08-30).

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🌠 Phenomenal Traffic: 5M - 10M visitors per month

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Keywords {🔍}

kinase, drp, article, protein, access, taylor, francis, log, dap, online, group, page, journals, search, register, cart, issue, apoptosis, catalytic, domain, pdf, content, add, cellular, deathassociated, kinaserelated, cell, homology, region, camregulatory, cterminal, induced, death, work, research, open, login, molecular, biology, volume, journal, citations, date, serinethreonine, published, reprints, read, zip, drak, shown,

Topics {✒️}

remaining c-terminal part serine/threonine kinase involved journals bioscience molecular downloaded article pdf francis group ca2+/cam-dependent manner downloaded article pdfs c-terminal tail limited period serine/threonine kinases block apoptosis induced 42-kda ca2+/calmodulin dominant negative manner institution access cellular biology list advanced search molecular apoptosis boaz inbal structure-function analysis shows high degree cellular fractionation assays myosin light chain dominant negative fragment expression vector carrying rfx-δsmai construct journals books receive personalised research protein kinase-related kinase-related protein constitutively active kinase protein differs completely catalytically inactive mutant ref death assays authors contributed equally helena rubinstein chair dap kinase encompassing cam-regulatory region mouse drp-1 homologues cam-regulatory domain cart search dap kinase drp-1 published online article https article abstract date register issue 3 death zip kinase register log cell killing cancer research dap kinase

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            name:Death-Associated Protein Kinase-Related ....
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ScholarlyArticle:
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      articleSection:Cell Growth and Development
      name:Death-Associated Protein Kinase-Related Protein 1, a Novel Serine/Threonine Kinase Involved in Apoptosis
      headline:Death-Associated Protein Kinase-Related Protein 1, a Novel Serine/Threonine Kinase Involved in Apoptosis
      abstract:In this study we describe the identification and structure-function analysis of a novel death-associated protein (DAP) kinase-related protein, DRP-1. DRP-1 is a 42-kDa Ca2+/calmodulin (CaM)-regulated serine threonine kinase which shows high degree of homology to DAP kinase. The region of homology spans the catalytic domain and the CaM-regulatory region, whereas the remaining C-terminal part of the protein differs completely from DAP kinase and displays no homology to any known protein. The catalytic domain is also homologous to the recently identified ZIP kinase and to a lesser extent to the catalytic domains of DRAK1 and -2. Thus, DAP kinase DRP-1, ZIP kinase, and DRAK1/2 together form a novel subfamily of serine/threonine kinases. DRP-1 is localized to the cytoplasm, as shown by immunostaining and cellular fractionation assays. It binds to CaM, undergoes autophosphorylation, and phosphorylates an exogenous substrate, the myosin light chain, in a Ca2+/CaM-dependent manner. The truncated protein, deleted of the CaM-regulatory domain, was converted into a constitutively active kinase. Ectopically expressed DRP-1 induced apoptosis in various types of cells. Cell killing by DRP-1 was dependent on two features: the status of the catalytic activity, and the presence of the C-terminal 40 amino acids shown to be required for self-dimerization of the kinase. Interestingly, further deletion of the CaM-regulatory region could override the indispensable role of the C-terminal tail in apoptosis and generated a “superkiller” mutant. A dominant negative fragment of DAP kinase encompassing the death domain was found to block apoptosis induced by DRP-1. Conversely, a catalytically inactive mutant of DRP-1, which functioned in a dominant negative manner, was significantly less effective in blocking cell death induced by DAP kinase. Possible functional connections between DAP kinase and DRP-1 are discussed.
      description:In this study we describe the identification and structure-function analysis of a novel death-associated protein (DAP) kinase-related protein, DRP-1. DRP-1 is a 42-kDa Ca2+/calmodulin (CaM)-regulated serine threonine kinase which shows high degree of homology to DAP kinase. The region of homology spans the catalytic domain and the CaM-regulatory region, whereas the remaining C-terminal part of the protein differs completely from DAP kinase and displays no homology to any known protein. The catalytic domain is also homologous to the recently identified ZIP kinase and to a lesser extent to the catalytic domains of DRAK1 and -2. Thus, DAP kinase DRP-1, ZIP kinase, and DRAK1/2 together form a novel subfamily of serine/threonine kinases. DRP-1 is localized to the cytoplasm, as shown by immunostaining and cellular fractionation assays. It binds to CaM, undergoes autophosphorylation, and phosphorylates an exogenous substrate, the myosin light chain, in a Ca2+/CaM-dependent manner. The truncated protein, deleted of the CaM-regulatory domain, was converted into a constitutively active kinase. Ectopically expressed DRP-1 induced apoptosis in various types of cells. Cell killing by DRP-1 was dependent on two features: the status of the catalytic activity, and the presence of the C-terminal 40 amino acids shown to be required for self-dimerization of the kinase. Interestingly, further deletion of the CaM-regulatory region could override the indispensable role of the C-terminal tail in apoptosis and generated a “superkiller” mutant. A dominant negative fragment of DAP kinase encompassing the death domain was found to block apoptosis induced by DRP-1. Conversely, a catalytically inactive mutant of DRP-1, which functioned in a dominant negative manner, was significantly less effective in blocking cell death induced by DAP kinase. Possible functional connections between DAP kinase and DRP-1 are discussed.
      author:
            type:Person
            name:Boaz Inbal
            type:Person
            name:Gidi Shani
            type:Person
            name:Ofer Cohen
            type:Person
            name:Joseph L. Kissil
            type:Person
            name:Adi Kimchi
      pageStart:1044
      pageEnd:1054
      datePublished:2023-03-28
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      name:Gidi Shani
      name:Ofer Cohen
      name:Joseph L. Kissil
      name:Adi Kimchi
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