scholarly journals Myristoylated alanine-rich C-kinase substrate effector domain phosphorylation regulates the growth and radiation sensitization of glioblastoma

2019 ◽  
Author(s):  
Nicholas Eustace ◽  
Joshua Anderson ◽  
Catherine Langford ◽  
Hoa Trummell ◽  
Patricia Hicks ◽  
...  
Keyword(s):  
Effector Domain ◽  
Kinase Substrate ◽  
Radiation Sensitization

scholarly journals The Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Binds Strongly to Phosphatidylinositol 4,5-Bisphosphate

2000 ◽  
Vol 276 (7) ◽  
pp. 5012-5019 ◽  
Author(s):  
Jiyao Wang ◽  
Anna Arbuzova ◽  
Gyöngyi Hangyás-Mihályné ◽  
Stuart McLaughlin
Keyword(s):  
Effector Domain ◽  
Kinase Substrate

scholarly journals Location of the Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Effector Domain in Negatively Charged Phospholipid Bicelles

2003 ◽  
Vol 85 (4) ◽  
pp. 2442-2448 ◽  
Author(s):  
Jeffrey F. Ellena ◽  
M. Christine Burnitz ◽  
David S. Cafiso
Keyword(s):  
Effector Domain ◽  
Kinase Substrate

scholarly journals Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes

1998 ◽  
Vol 330 (1) ◽  
pp. 5-11 ◽  
Author(s):  
Guy VERGÈRES ◽  
J. Jeremy RAMSDEN
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipid Vesicles ◽  
Related Protein ◽  
Effector Domain ◽  
Lower Affinity ◽  
Kinase Substrate ◽  
Kinase C ◽  
Central Effector

The myristoylated alanine-rich C kinase substrate (MARCKS) protein family has two known members, MARCKS itself and MARCKS-related protein (MRP, also called MacMARCKS or F52). They are essential for brain development and are believed to regulate the structure of the actin cytoskeleton at the plasma membrane. Hence membrane binding is central to their function. MARCKS has been quite extensively characterized; MRP much less so. Despite the fact that MRP is only two thirds the size of MARCKS, it has hitherto been assumed that the two proteins have similar properties. Here we make a detailed study, including the effects of myristoylation, lipid composition, calmodulin and phosphorylation of the binding of MRP to phospholipid vesicles. We show that both the N-terminal myristoyl moiety and the central effector domain mediate binding. MRP behaves like MARCKS in the presence of neutral phospholipids. In contrast to MARCKS, however, the incorporation of 20% of negatively-charged phospholipids only marginally increases the affinity of myristoylated MRP. Co-operativity between the myristoyl moiety and the effector domain of MRP is weak and the protein has a significantly lower affinity for these vesicles compared with MARCKS. Furthermore, calmodulin or phosphorylation of the effector domain by the catalytic subunit of protein kinase C do not significantly decrease the binding of myristoylated MRP to negatively-charged phospholipid vesicles. Our results show that the mechanisms regulating the interactions of MARCKS and MRP with phospholipid vesicles are, at least quantitatively, different. In agreement with cellular studies, we therefore propose that MARCKS and MRP have different subcellular localization and, consequently, different functions.

scholarly journals Lateral Sequestration of Phosphatidylinositol 4,5-Bisphosphate by the Basic Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Is Due to Nonspecific Electrostatic Interactions

2002 ◽  
Vol 277 (37) ◽  
pp. 34401-34412 ◽  
Author(s):  
Jiyao Wang ◽  
Alok Gambhir ◽  
Gyöngyi Hangyás-Mihályné ◽  
Diana Murray ◽  
Urszula Golebiewska ◽  
...  
Keyword(s):  
Electrostatic Interactions ◽  
Effector Domain ◽  
Kinase Substrate

scholarly journals Targeting the effector domain of the myristoylated alanine rich C-kinase substrate enhances lung cancer radiation sensitivity

2014 ◽  
Vol 46 (3) ◽  
pp. 1079-1088 ◽  
Author(s):  
TIMOTHY D. ROHRBACH ◽  
JOHN S. JARBOE ◽  
JOSHUA C. ANDERSON ◽  
HOA Q. TRUMMELL ◽  
PATRICIA H. HICKS ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Radiation Sensitivity ◽  
Effector Domain ◽  
Kinase Substrate

Cross-talk unfolded: MARCKS proteins

2002 ◽  
Vol 362 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Anna ARBUZOVA ◽  
Arndt A. P. SCHMITZ ◽  
Guy VERGÈRES
Keyword(s):  
Actin Cytoskeleton ◽  
Cross Talk ◽  
Protein Modification ◽  
Membrane Binding ◽  
Point Of View ◽  
Cellular Migration ◽  
Effector Domain ◽  
Kinase Substrate ◽  
Natively Unfolded

The proteins of the MARCKS (myristoylated alanine-rich C kinase substrate) family were first identified as prominent substrates of protein kinase C (PKC). Since then, these proteins have been implicated in the regulation of brain development and postnatal survival, cellular migration and adhesion, as well as endo-, exo- and phago-cytosis, and neurosecretion. The effector domain of MARCKS proteins is phosphorylated by PKC, binds to calmodulin and contributes to membrane binding. This multitude of mutually exclusive interactions allows cross-talk between the signal transduction pathways involving PKC and calmodulin. This review focuses on recent, mostly biophysical and biochemical results renewing interest in this protein family. MARCKS membrane binding is now understood at the molecular level. From a structural point of view, there is a consensus emerging that MARCKS proteins are ‘natively unfolded'. Interestingly, domains similar to the effector domain have been discovered in other proteins. Furthermore, since the effector domain enhances the polymerization of actin in vitro, MARCKS proteins have been proposed to mediate regulation of the actin cytoskeleton. However, the recent observations that MARCKS might serve to sequester phosphatidylinositol 4,5-bisphosphate in the plasma membrane of unstimulated cells suggest an alternative model for the control of the actin cytoskeleton. While myristoylation is classically considered to be a co-translational, irreversible event, new reports on MARCKS proteins suggest a more dynamic picture of this protein modification. Finally, studies with mice lacking MARCKS proteins have investigated the functions of these proteins during embryonic development in the intact organism.

Myristoylated alanine‐rich C‐kinase substrate effector domain peptide improves sex‐specific recovery and axonal regrowth after spinal cord injury

2020 ◽  
Vol 34 (9) ◽  
pp. 12677-12690
Author(s):  
Thomas Theis ◽  
Suneel Kumar ◽  
Elena Wei ◽  
Jennifer Nguyen ◽  
Vicci Glynos ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Spinal Cord Injury ◽  
Effector Domain ◽  
Kinase Substrate ◽  
Axonal Regrowth ◽  
Cord Injury ◽  
Domain Peptide
Sign in / Sign up

Export Citation Format

Share Document