Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo (Record no. 42482)

MARC details
000 -LEADER
fixed length control field 02257nam a2200253Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625124715.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-8176
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 250602s9999 xx |||||s2 |||| ||und|d
245 10 - TITLE STATEMENT
Title Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo
490 0# - SERIES STATEMENT
Volume/sequential designation Cellular Signalling, 18(1), p.123-134, 2006
520 3# - SUMMARY, ETC.
Summary, etc. Docking sites on targets of mitogen-activated protein kinases (MAPKs)facilitate accurate and efficient substrate phosphorylation. MAPK/ ERK kinases (MEKs, or MKKs), the upstream regulators of MAPKs, also contain N-terminal MAPK-docking sites, or FD-sites_; however, the in vivo functions of MEK D-sites are incompletely understood. Here we found that the ability of constitutively-active human MEK1 and MEK2 to stimulate ERK phosphorylation and to induce the neoplastic transformation of NIH 3T3 cells required the integrity of the D-site. In addition, D-site mutants of otherwise wild-type MEK1/2 were unable to anchor unphosphorylated ERK2 in the cytoplasm. ERK activation, cytoplasmic anchoring and release were completely retained in Fswap_ mutants in which MEK2's D-site was replaced with the D-site of MEK1 or yeast Ste7. Furthermore, these abilities were significantly retained when MEK2's D-site was moved to its C-terminus, or replaced by an unrelated MAPK-binding domain taken from the Ets-1 transcription factor. We conclude that the D-sites in MEKs are crucial for the activation of their cognate MAPKs in vivo, and that their primary function is to tether their cognate MAPKs near the MEK's kinase domain. This proximity effect is sufficient to explain the contribution that the D-site interaction makes to several biologically important signaling events
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element MITOGEN-ACTIVATED PROTEIN KINASES
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element SIGNAL TRANSDUCTION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PHOSPHORYLATION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element BINDING SITES
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PROTEIN BINDING
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Grewal, S.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Molina, D.M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Bardwell, L.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/18pmwQ_x38R8ZMAuEO-PhvLltpK1LcesO/view?usp=drivesdk">https://drive.google.com/file/d/18pmwQ_x38R8ZMAuEO-PhvLltpK1LcesO/view?usp=drivesdk</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
Holdings
Lost status Source of classification or shelving scheme Damaged status Not for loan Collection Home library Current library Shelving location Date acquired Total checkouts Full call number Date last seen Price effective from Koha item type
  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-8176 25.06.2025 25.06.2025 Documentos solicitados