Phosphatidylinositol 4,5-bisphosphate is regenerated by speeding of the PI 4-kinase pathway during long PLC activation

The dynamic metabolism of membrane phosphoinositide lipids involves several cellular compartments including the ER, Golgi, and plasma membrane. There are cycles of phosphorylation and dephosphorylation and of synthesis, transfer, and breakdown. The simplified phosphoinositide cycle comprises synthes...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of general physiology Vol. 152; no. 12
Main Authors: Myeong, Jongyun, de la Cruz, Lizbeth, Jung, Seung-Ryoung, Yeon, Jun-Hee, Suh, Byung-Chang, Koh, Duk-Su, Hille, Bertil
Format: Journal Article
Language:English
Published: 07.12.2020
ISSN:1540-7748, 1540-7748
Online Access:Get more information
Tags: Add Tag
No Tags, Be the first to tag this record!
Abstract The dynamic metabolism of membrane phosphoinositide lipids involves several cellular compartments including the ER, Golgi, and plasma membrane. There are cycles of phosphorylation and dephosphorylation and of synthesis, transfer, and breakdown. The simplified phosphoinositide cycle comprises synthesis of phosphatidylinositol in the ER, transport, and phosphorylation in the Golgi and plasma membranes to generate phosphatidylinositol 4,5-bisphosphate, followed by receptor-stimulated hydrolysis in the plasma membrane and return of the components to the ER for reassembly. Using probes for specific lipid species, we have followed and analyzed the kinetics of several of these events during stimulation of M1 muscarinic receptors coupled to the G-protein Gq. We show that during long continued agonist action, polyphosphorylated inositol lipids are initially depleted but then regenerate while agonist is still present. Experiments and kinetic modeling reveal that the regeneration results from gradual but massive up-regulation of PI 4-kinase pathways rather than from desensitization of receptors. Golgi pools of phosphatidylinositol 4-phosphate and the lipid kinase PI4KIIIα (PI4KA) contribute to this homeostatic regeneration. This powerful acceleration, which may be at the level of enzyme activity or of precursor and product delivery, reveals strong regulatory controls in the phosphoinositide cycle.The dynamic metabolism of membrane phosphoinositide lipids involves several cellular compartments including the ER, Golgi, and plasma membrane. There are cycles of phosphorylation and dephosphorylation and of synthesis, transfer, and breakdown. The simplified phosphoinositide cycle comprises synthesis of phosphatidylinositol in the ER, transport, and phosphorylation in the Golgi and plasma membranes to generate phosphatidylinositol 4,5-bisphosphate, followed by receptor-stimulated hydrolysis in the plasma membrane and return of the components to the ER for reassembly. Using probes for specific lipid species, we have followed and analyzed the kinetics of several of these events during stimulation of M1 muscarinic receptors coupled to the G-protein Gq. We show that during long continued agonist action, polyphosphorylated inositol lipids are initially depleted but then regenerate while agonist is still present. Experiments and kinetic modeling reveal that the regeneration results from gradual but massive up-regulation of PI 4-kinase pathways rather than from desensitization of receptors. Golgi pools of phosphatidylinositol 4-phosphate and the lipid kinase PI4KIIIα (PI4KA) contribute to this homeostatic regeneration. This powerful acceleration, which may be at the level of enzyme activity or of precursor and product delivery, reveals strong regulatory controls in the phosphoinositide cycle.
AbstractList The dynamic metabolism of membrane phosphoinositide lipids involves several cellular compartments including the ER, Golgi, and plasma membrane. There are cycles of phosphorylation and dephosphorylation and of synthesis, transfer, and breakdown. The simplified phosphoinositide cycle comprises synthesis of phosphatidylinositol in the ER, transport, and phosphorylation in the Golgi and plasma membranes to generate phosphatidylinositol 4,5-bisphosphate, followed by receptor-stimulated hydrolysis in the plasma membrane and return of the components to the ER for reassembly. Using probes for specific lipid species, we have followed and analyzed the kinetics of several of these events during stimulation of M1 muscarinic receptors coupled to the G-protein Gq. We show that during long continued agonist action, polyphosphorylated inositol lipids are initially depleted but then regenerate while agonist is still present. Experiments and kinetic modeling reveal that the regeneration results from gradual but massive up-regulation of PI 4-kinase pathways rather than from desensitization of receptors. Golgi pools of phosphatidylinositol 4-phosphate and the lipid kinase PI4KIIIα (PI4KA) contribute to this homeostatic regeneration. This powerful acceleration, which may be at the level of enzyme activity or of precursor and product delivery, reveals strong regulatory controls in the phosphoinositide cycle.The dynamic metabolism of membrane phosphoinositide lipids involves several cellular compartments including the ER, Golgi, and plasma membrane. There are cycles of phosphorylation and dephosphorylation and of synthesis, transfer, and breakdown. The simplified phosphoinositide cycle comprises synthesis of phosphatidylinositol in the ER, transport, and phosphorylation in the Golgi and plasma membranes to generate phosphatidylinositol 4,5-bisphosphate, followed by receptor-stimulated hydrolysis in the plasma membrane and return of the components to the ER for reassembly. Using probes for specific lipid species, we have followed and analyzed the kinetics of several of these events during stimulation of M1 muscarinic receptors coupled to the G-protein Gq. We show that during long continued agonist action, polyphosphorylated inositol lipids are initially depleted but then regenerate while agonist is still present. Experiments and kinetic modeling reveal that the regeneration results from gradual but massive up-regulation of PI 4-kinase pathways rather than from desensitization of receptors. Golgi pools of phosphatidylinositol 4-phosphate and the lipid kinase PI4KIIIα (PI4KA) contribute to this homeostatic regeneration. This powerful acceleration, which may be at the level of enzyme activity or of precursor and product delivery, reveals strong regulatory controls in the phosphoinositide cycle.
Author Koh, Duk-Su
Suh, Byung-Chang
Yeon, Jun-Hee
Jung, Seung-Ryoung
Myeong, Jongyun
Hille, Bertil
de la Cruz, Lizbeth
Author_xml – sequence: 1
  givenname: Jongyun
  surname: Myeong
  fullname: Myeong, Jongyun
– sequence: 2
  givenname: Lizbeth
  surname: de la Cruz
  fullname: de la Cruz, Lizbeth
– sequence: 3
  givenname: Seung-Ryoung
  surname: Jung
  fullname: Jung, Seung-Ryoung
– sequence: 4
  givenname: Jun-Hee
  surname: Yeon
  fullname: Yeon, Jun-Hee
– sequence: 5
  givenname: Byung-Chang
  surname: Suh
  fullname: Suh, Byung-Chang
– sequence: 6
  givenname: Duk-Su
  surname: Koh
  fullname: Koh, Duk-Su
– sequence: 7
  givenname: Bertil
  surname: Hille
  fullname: Hille, Bertil
BookMark eNpNUD1PwzAQtVCRaAsju0cGUmzXH-mIKiiVKtEB5sqxL41LsEPsFPXfY1QGbnj33runO-kmaOSDB4RuKZlRUoqHw76bMcIIZZKpCzSmgpNCKV6O_vErNInxQHIJRsbouG1C7BqdnD21zofoUmgxvxdF5bJ_ngF2EfewBw99VhZXJxw7AOv8Hocapwbwdo158eG8joA7nZpvfcJ26H8Tbciw3SyxNskd86ngr9FlrdsIN399it6fn96WL8XmdbVePm4Kw0WZClHVQsh5panUUFuqWWWosZIbq6Dk3NIFVVKVSghqS-BS5mTNDK9k9uoFm6K7896uD18DxLT7dNFA22oPYYg7xiVRks_zM34AjaFiWQ
CitedBy_id crossref_primary_10_1073_pnas_2202926119
crossref_primary_10_1016_j_bbalip_2025_159615
crossref_primary_10_1073_pnas_2025343118
crossref_primary_10_3389_fphar_2021_663840
crossref_primary_10_1016_j_ceb_2021_03_004
crossref_primary_10_1007_s00424_023_02834_8
crossref_primary_10_3390_membranes11050339
crossref_primary_10_1016_j_ceb_2023_102207
crossref_primary_10_1242_jcs_261494
crossref_primary_10_1016_j_jlr_2023_100480
crossref_primary_10_1016_j_bprint_2022_e00234
crossref_primary_10_1016_j_bbalip_2021_158985
crossref_primary_10_1242_jcs_259145
crossref_primary_10_1242_jcs_259365
crossref_primary_10_1073_pnas_2113852118
ContentType Journal Article
Copyright 2020 Myeong et al.
Copyright_xml – notice: 2020 Myeong et al.
DBID 7X8
DOI 10.1085/jgp.202012627
DatabaseName MEDLINE - Academic
DatabaseTitle MEDLINE - Academic
DatabaseTitleList MEDLINE - Academic
Database_xml – sequence: 1
  dbid: 7X8
  name: MEDLINE - Academic
  url: https://search.proquest.com/medline
  sourceTypes: Aggregation Database
DeliveryMethod no_fulltext_linktorsrc
Discipline Anatomy & Physiology
EISSN 1540-7748
GroupedDBID ---
-DZ
-~X
123
18M
29K
2WC
36B
4.4
5RE
5VS
79B
7X8
85S
ACGFO
ACGOD
ACIWK
ACNCT
ACPRK
ADBBV
AENEX
AHMBA
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BAWUL
BKOMP
BTFSW
C45
CS3
D-I
D0L
DIK
DU5
E3Z
EBS
EMB
F5P
F9R
GX1
H13
HF~
HYE
KQ8
L7B
O5R
O5S
OK1
P2P
PQQKQ
RHI
RXW
SJN
TAE
TR2
TRP
TWZ
UHB
UPT
W8F
WH7
WOQ
YKV
YOC
YQT
YSK
YWH
YZZ
ZCA
ID FETCH-LOGICAL-c458t-5bf5563ba16aefd1a2bc1cd64cd7e844d19176787551d8e466a16f2c4b6875f92
IEDL.DBID 7X8
ISICitedReferencesCount 17
ISICitedReferencesURI http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000599856200001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN 1540-7748
IngestDate Wed Oct 01 14:49:52 EDT 2025
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 12
Language English
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c458t-5bf5563ba16aefd1a2bc1cd64cd7e844d19176787551d8e466a16f2c4b6875f92
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
OpenAccessLink https://pubmed.ncbi.nlm.nih.gov/PMC7671494
PQID 2460764305
PQPubID 23479
ParticipantIDs proquest_miscellaneous_2460764305
PublicationCentury 2000
PublicationDate 2020-12-07
PublicationDateYYYYMMDD 2020-12-07
PublicationDate_xml – month: 12
  year: 2020
  text: 2020-12-07
  day: 07
PublicationDecade 2020
PublicationTitle The Journal of general physiology
PublicationYear 2020
SSID ssj0000520
Score 2.431219
Snippet The dynamic metabolism of membrane phosphoinositide lipids involves several cellular compartments including the ER, Golgi, and plasma membrane. There are...
SourceID proquest
SourceType Aggregation Database
Title Phosphatidylinositol 4,5-bisphosphate is regenerated by speeding of the PI 4-kinase pathway during long PLC activation
URI https://www.proquest.com/docview/2460764305
Volume 152
WOSCitedRecordID wos000599856200001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText
inHoldings 1
isFullTextHit
isPrint
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LS8NAEF7UevDiq4pvRhBPLm3TzSY5SSkWBSk9KPRW9tlWa1KbWum_d3aT0oMXwUsImz2E7GTmm9lvvyHkhnGDQbUeU7wJKUtsSGNlFBXoj7WME1MX0jebiLrduN9PemXBLS9plSuf6B21zpSrkdcCxjHldgJV99NP6rpGud3VsoXGJqk0Eco4q476a7Vwx_HweqmONRexuNTYRJRRexs6sUqMfgEPol9-2AeXzt5_X2uf7JawElqFHRyQDZMekmorxZT6Ywm34ImevoJeJYveKMunI1wSvUSQ6Vhb2QTYXYhZMo4XzwyMc5iZoVelRlQKcgn5tAh1kFlA3Ai9J2D0fZxiIATX2fhbLKE49giTDC-95za4cxNF1feIvHYeXtqPtGy_QBUL4zkNpXXqYVI0uDBWN0QgVUNpzpSOTMyYdqkexroIQZeODeMcZ9pAMclxzCbBMdlKs9ScEAhlIurcNkVDIPwyLBFJKIyuW2uY5lKekuvV1x2gebs9C5Ga7CsfrL_v2R_mnJMdt6iebhJdkIrFX9hckm21mI_z2ZW3jh9RKcbz
linkProvider ProQuest
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Phosphatidylinositol+4%2C5-bisphosphate+is+regenerated+by+speeding+of+the+PI+4-kinase+pathway+during+long+PLC+activation&rft.jtitle=The+Journal+of+general+physiology&rft.au=Myeong%2C+Jongyun&rft.au=de+la+Cruz%2C+Lizbeth&rft.au=Jung%2C+Seung-Ryoung&rft.au=Yeon%2C+Jun-Hee&rft.date=2020-12-07&rft.issn=1540-7748&rft.eissn=1540-7748&rft.volume=152&rft.issue=12&rft_id=info:doi/10.1085%2Fjgp.202012627&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1540-7748&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1540-7748&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1540-7748&client=summon