PMID- 22155644
OWN - NLM
STAT- MEDLINE
DCOM- 20120424
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1818
IP  - 3
DP  - 2012 Mar
TI  - Regulation of plasma membrane Ca(2+)-ATPase activity by acetylated tubulin: 
      influence of the lipid environment.
PG  - 601-8
LID - 10.1016/j.bbamem.2011.11.022 [doi]
AB  - We demonstrated previously that acetylated tubulin inhibits plasma membrane 
      Ca(2+)-ATPase (PMCA) activity in plasma membrane vesicles (PMVs) of rat brain 
      through a reversible interaction. Dissociation of the PMCA/tubulin complex leads 
      to restoration of ATPase activity. We now report that, when the enzyme is 
      reconstituted in phosphatidylcholine vesicles containing acidic or neutral 
      lipids, tubulin not only loses its inhibitory effect but is also capable of 
      activating PMCA. This alteration of the PMCA-inhibitory effect of tubulin was 
      dependent on concentrations of both lipids and tubulin. Tubulin (300mug/ml) in 
      combination with acidic lipids at concentrations >10%, increased PMCA activity up 
      to 27-fold. The neutral lipid diacylglycerol (DAG), in combination with 50mug/ml 
      tubulin, increased PMCA activity >12-fold, whereas tubulin alone at high 
      concentration (>/=300mug/ml) produced only 80% increase. When DAG was generated in 
      situ by phospholipase C incubation of PMVs pre-treated with exogenous tubulin, 
      the inhibitory effect of tubulin on PMCA activity (ATP hydrolysis, and Ca(2+) 
      transport within vesicles) was reversed. These findings indicate that PMCA is 
      activated independently of surrounding lipid composition at low tubulin 
      concentrations (<50mug/ml), whereas PMCA is activated mainly by reconstitution in 
      acidic lipids at high tubulin concentrations. Regulation of PMCA activity by 
      tubulin is thus dependent on both membrane lipid composition and tubulin 
      concentration.
CI  - Copyright (c) 2011 Elsevier B.V. All rights reserved.
FAU - Monesterolo, N E
AU  - Monesterolo NE
AD  - Departamento de Biologia Molecular, Universidad Nacional de Rio Cuarto, 
      Argentina.
FAU - Amaiden, M R
AU  - Amaiden MR
FAU - Campetelli, A N
AU  - Campetelli AN
FAU - Santander, V S
AU  - Santander VS
FAU - Arce, C A
AU  - Arce CA
FAU - Pie, J
AU  - Pie J
FAU - Casale, C H
AU  - Casale CH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20111203
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Membrane Lipids)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Tubulin)
RN  - EC 3.1.4.- (Type C Phospholipases)
RN  - EC 3.6.3.8 (Plasma Membrane Calcium-Transporting ATPases)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Acetylation
MH  - Animals
MH  - Brain/metabolism
MH  - Brain Chemistry/physiology
MH  - Calcium/*metabolism
MH  - Cell Membrane/chemistry/*enzymology
MH  - Ion Transport/physiology
MH  - Membrane Lipids/chemistry/*metabolism
MH  - Nerve Tissue Proteins/chemistry/*metabolism
MH  - Plasma Membrane Calcium-Transporting ATPases/chemistry/*metabolism
MH  - Rats
MH  - Tubulin/chemistry/*metabolism
MH  - Type C Phospholipases/chemistry
EDAT- 2011/12/14 06:00
MHDA- 2012/04/25 06:00
CRDT- 2011/12/14 06:00
PHST- 2011/06/02 00:00 [received]
PHST- 2011/11/15 00:00 [revised]
PHST- 2011/11/22 00:00 [accepted]
PHST- 2011/12/14 06:00 [entrez]
PHST- 2011/12/14 06:00 [pubmed]
PHST- 2012/04/25 06:00 [medline]
AID - S0005-2736(11)00412-3 [pii]
AID - 10.1016/j.bbamem.2011.11.022 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2012 Mar;1818(3):601-8. doi: 10.1016/j.bbamem.2011.11.022. 
      Epub 2011 Dec 3.