Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.11.11 (
AMPK
)
12,425
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Activities of many proteins including protein kinases are often regulated by their dynamic association with specific intracellular compartments.
MAK-V
is an
AMPK
-like protein kinase with poorly characterized functions and mechanisms of action. Similarly to many other protein kinases, association of
MAK-V
with specific intracellular compartments could be essential for its proper functions. In this work, we studied subcellular distribution of exogenously produced and endogenous
MAK-V
proteins in mammalian cells using biochemical cell fractioning aiming to supplement data on
MAK-V
intracellular localization studied by immunocytochemical methods. We found that a significant portion of
MAK-V
protein in mammalian cells is associated with membranes. Moreover,
MAK-V
expressed in yeast was also targeted to membrane, thus suggesting an evolutionarily conservative mechanism of
MAK-V
membrane association. Based on the ability of various
MAK-V
deletion mutants to localize to membrane and comparison of
MAK-V
amino acid sequences from different species, we suggest a possible mechanism governing
MAK-V
association with intracellular membranes.
...
PMID:Membrane localization of the MAK-V protein kinase. 1839 62
MAK-V
/Hunk is a scantily characterized
AMPK
-like protein kinase. Recent findings identified
MAK-V
as a pro-survival and anti-apoptotic protein and revealed its role in embryonic development as well as in tumorigenesis and metastasis. However molecular mechanisms of
MAK-V
action and regulation of its activity remain largely unknown. We identified Nedd4 as an interaction partner for
MAK-V
protein kinase. However, this HECT-type E3 ubiquitin ligase is not involved in the control of
MAK-V
degradation by the ubiquitin-proteasome system that regulates
MAK-V
abundance in cells. However, Nedd4 in an ubiquitin ligase-independent manner rescued developmental defects in Xenopus embryos induced by
MAK-V
overexpression, suggesting physiological relevance of interaction between
MAK-V
and Nedd4. This identifies Nedd4 as the first known regulator of
MAK-V
function.
...
PMID:Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase. 2274 72
