BAIT

MARCKS

80K-L, MACS, PKCSL, PRKCSL
myristoylated alanine-rich protein kinase C substrate
GO Process (3)
GO Function (1)
GO Component (4)
Homo sapiens

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

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

Eustace NJ, Anderson JC, Langford CP, Trummell HQ, Hicks PH, Jarboe JS, Mobley JA, Hjelmeland AB, Hackney JR, Pedersen RT, Cosby K, Gillespie GY, Bonner JA, Willey CD

Glioblastoma harbors frequent alterations in receptor tyrosine kinases, phosphatidylinositol?3 kinase (PI3K) and phosphatase and tensin homolog (PTEN) that dysregulate phospholipid signaling driven tumor proliferation and therapeutic resistance. Myristoylated alanine?rich C?kinase substrate (MARCKS) is a 32 kDa intrinsically unstructured protein containing a polybasic (+13) effector domain (ED), which regulates its electrostatic sequestration of phospholipid phosphatidylinositol (4,5)?bisphosphate (PIP2), and its binding to phosphatidylserine, calcium/calmodulin, filamentous actin, while ... [more]

Int. J. Oncol. Jun. 01, 2019; 54(6);2039-2053 [Pubmed: 30942445]

Throughput

  • Low Throughput

Curated By

  • BioGRID