Kisseleva MV artikkeleita PubMed haku

 

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1

The role of phosphatases in inositol signaling reactions.

Majerus PW, Kisseleva MV, Norris FA. J Biol Chem. 1999 Apr 16;274(16):10669-72. doi: 10.1074/jbc.274.16.10669. PMID: 10196133 Free article. Review. No abstract available.

2

The role of inositol signaling in the control of apoptosis.

Majerus PW, Zou J, Marjanovic J, Kisseleva MV, Wilson MP. Adv Enzyme Regul. 2008;48:10-7. doi: 10.1016/j.advenzreg.2008.04.001. Epub 2008 Apr 29. PMID: 18486622 Free PMC article. No abstract available.

3

Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis.

Zou J, Marjanovic J, Kisseleva MV, Wilson M, Majerus PW. Proc Natl Acad Sci U S A. 2007 Oct 23;104(43):16834-9. doi: 10.1073/pnas.0708189104. Epub 2007 Oct 16. PMID: 17940011 Free PMC article.

4

Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies.

Bielas SL, Silhavy JL, Brancati F, Kisseleva MV, Al-Gazali L, Sztriha L, Bayoumi RA, Zaki MS, Abdel-Aleem A, Rosti RO, Kayserili H, Swistun D, Scott LC, Bertini E, Boltshauser E, Fazzi E, Travaglini L, Field SJ, Gayral S, Jacoby M, Schurmans S, Dallapiccola B, Majerus PW, Valente EM, Gleeson JG. Nat Genet. 2009 Sep;41(9):1032-6. doi: 10.1038/ng.423. Epub 2009 Aug 9. PMID: 19668216 Free PMC article.

5

Myotubularin-related protein (MTMR) 9 determines the enzymatic activity, substrate specificity, and role in autophagy of MTMR8.

Zou J, Zhang C, Marjanovic J, Kisseleva MV, Majerus PW, Wilson MP. Proc Natl Acad Sci U S A. 2012 Jun 12;109(24):9539-44. doi: 10.1073/pnas.1207021109. Epub 2012 May 30. PMID: 22647598 Free PMC article.

6

INPP5E mutations cause primary cilium signaling defects, ciliary instability and ciliopathies in human and mouse.

Jacoby M, Cox JJ, Gayral S, Hampshire DJ, Ayub M, Blockmans M, Pernot E, Kisseleva MV, Compère P, Schiffmann SN, Gergely F, Riley JH, Pérez-Morga D, Woods CG, Schurmans S. Nat Genet. 2009 Sep;41(9):1027-31. doi: 10.1038/ng.427. Epub 2009 Aug 9. PMID: 19668215 Free article.

7

The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase.

Verbsky JW, Wilson MP, Kisseleva MV, Majerus PW, Wente SR. J Biol Chem. 2002 Aug 30;277(35):31857-62. doi: 10.1074/jbc.M205682200. Epub 2002 Jun 25. PMID: 12084730 Free article.

8

The isolation and characterization of a cDNA encoding phospholipid-specific inositol polyphosphate 5-phosphatase.

Kisseleva MV, Wilson MP, Majerus PW. J Biol Chem. 2000 Jun 30;275(26):20110-6. doi: 10.1074/jbc.M910119199. PMID: 10764818 Free article.

9

The type Ialpha inositol polyphosphate 4-phosphatase generates and terminates phosphoinositide 3-kinase signals on endosomes and the plasma membrane.

Ivetac I, Munday AD, Kisseleva MV, Zhang XM, Luff S, Tiganis T, Whisstock JC, Rowe T, Majerus PW, Mitchell CA. Mol Biol Cell. 2005 May;16(5):2218-33. doi: 10.1091/mbc.e04-09-0799. Epub 2005 Feb 16. PMID: 15716355 Free PMC article.

10

Phosphoinositide-specific inositol polyphosphate 5-phosphatase IV inhibits Akt/protein kinase B phosphorylation and leads to apoptotic cell death.

Kisseleva MV, Cao L, Majerus PW. J Biol Chem. 2002 Feb 22;277(8):6266-72. doi: 10.1074/jbc.M105969200. Epub 2001 Nov 12. PMID: 11706019 Free article.

Ooms L et al. Inositolipolyfosfaattien 5-aseman fosfataaseja on kymmenen: ( IPx-5-ptases)

 Inositolipolyfosfaattien 5- aseman fosfataasien joukossa on  5-ptaasiIV joka on ppfsfpinositidi PI(3,4,5)P3 spesifinen ja  vaikuttaa myös PI(4,5)P2, muotoon, jolloin produktit ovat  PI(3,4)P2 ja PI(4)P.  Tämä  vaikuttaa  tasapainonmuutosta PI3K- kinaasin produktien  kesken: (PI(3,4,5)P3 ja PI(3,4)P2 ja samalla PKB/AKT-signalointitiehen) (Kisseleva MV  kirjoitti asiasta 2002  seuraavassa 10 kpl Kisselevan artikkeleita PubMedistä).

 Document: Current.  

Lisa Ooms et al. 2009 

 Abstract: Review Article| March 13 2009

The role of the inositol polyphosphate 5-phosphatases in cellular function and human disease

DOI: 10.1042/BJ20081673  

Phosphoinositides are membrane-bound signalling molecules that regulate cell proliferation and survival, cytoskeletal reorganization and vesicular trafficking by recruiting effector proteins to cellular membranes. Growth factor or insulin stimulation induces a canonical cascade resulting in the transient phosphorylation of PtdIns(4,5)P₂ by PI3K (phosphoinositide 3-kinase) to form PtdIns(3,4,5)P₃, which is rapidly dephosphorylated either by PTEN (phosphatase and tensin homologue deleted on chromosome 10) back to PtdIns(4,5)P₂, or by the 5-ptases (inositol polyphosphate 5-phosphatases), generating PtdIns(3,4)P₂. The 5-ptases also hydrolyse PtdIns(4,5)P₂, forming PtdIns4P. Ten mammalian 5-ptases have been identified, which share a catalytic mechanism similar to that of the apurinic/apyrimidinic endonucleases. Gene-targeted deletion of 5-ptases in mice has revealed that these enzymes regulate haemopoietic cell proliferation, synaptic vesicle recycling, insulin signalling, endocytosis, vesicular trafficking and actin polymerization. Several studies have revealed that the molecular basis of Lowe's syndrome is due to mutations in the 5-ptase OCRL (oculocerebrorenal syndrome of Lowe). Futhermore, the 5-ptases SHIP [SH2 (Src homology 2)-domain-containing inositol phosphatase] 2, SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) and 72-5ptase (72 kDa 5-ptase)/Type IV/Inpp5e (inositol polyphosphate 5-phosphatase E) are implicated in negatively regulating insulin signalling and glucose homoeostasis in specific tissues. SHIP2 polymorphisms are associated with a predisposition to insulin resistance. Gene profiling studies have identified changes in the expression of various 5-ptases in specific cancers. In addition, 5-ptases such as SHIP1, SHIP2 and 72-5ptase/Type IV/Inpp5e regulate macrophage phagocytosis, and SHIP1 also controls haemopoietic cell proliferation. Therefore the 5-ptases are a significant family of signal-modulating enzymes that govern a plethora of cellular functions by regulating the levels of specific phosphoinositides. Emerging studies have implicated their loss or gain of function in human disease. 

Annexiini A2 toimii myeliinialueellakin ja on membraaniappositiossa apuna (2022 tietoa)

  https://doi.org/10.3390/cells9020470

 

Huomaa: Myeliini on  hermojen kaapeliainetat ja sen takia siinä ei ole inositolijärjestelmän nopeasti vaihtuvia ja impulssikehitystä  ja energiamuodostusta  tukevia modulijäseniä  niin  merkattu esiin. Siihen sen sijaan uppotuu  pitkn kestäiä  rakenteita, jotka tietysti uusiutuat pikkuhiljaa, koska aivomodulilla on se  rasvarakenteittensa  puoliintumisaika ja uusiintumisaikansa. 

 Sen sijaan neuronien puoella  signaalia  lähettävissä  terminaalei ja energian generaattorikohdissa kyllä niitä PI-lipidiaineita  havaitaan.  runsaammin:  Harmaan aineen soluissa. Otan tähän fytiiniblogiin mukaan  myeliinin    kaapelirakenteen  korostaakseni että inositolipideillä on ietty oma modulinsa  joka toimii  kalvojärjestelmän ja sytoplasman  rajapinnoissa energian kehityksessä ja  signaalien  aikaansaamisessa. Niitten  molekyylien toimintasykli on nopeahkoa.  Myös haiman  harmaiden saarekkeiden  soluilla on  samantapaista  inositoli-lipidien ja inositolipolyfosfaattien modulin toimintaa-   energiatarkoituksiin koko keholle ja  energiainetta  aivojen tarpeisiin  tuottamiseen, koska neuronien energiatarve on jatkuva ja  neuronin resurssit toimia metabolisesti ovat  rajalliset. . 

Mitkondrioilla,  joilla on oma  DNA:nsa mtDNA, on myös omanlaatuisensa  kalvolipidi kardiolipiini, jota ei ole aivorakenteissa eikä  haimassa muuta kuin  solujen  mitokondrioissa ( ja niiden kalvojärjestelmissä sijaitsee  mm.  ihmisen energialaitos). 

Onko  annexiineillä jotakin osuutta  kardiolipiinissäkin, kun  annexeenja on toista tuhatta  muissakin kuin selkärankaisissa. saattaa olla, mutta ei niitä  ANX  A-tyyppisiä, vertebrata tyyppisiä, luulisin.  Ihmisen oman DNA:n koodaama ANXA voi ilmeisesti translokoitua mitokondraian ja aiheutaa apoptoosin kuten ANX5  ( https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4256031/).

 

 

 

Annexin A2 (ANXA2) sitoutuu PI (4,5)P2 -fosfatidylinositidilajiin solun cytokineesin alkutapahtumissa.

 

• Rescher U, Ruhe D, Ludwig C, Zobiack N, Gerke V (2004) Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J Cell Sci 117: 3473–3480CrossrefCASPubMedWeb of Science®Google Scholar

• Janetopoulos C, Devreotes P (2006) Phosphoinositide signaling plays a key role in cytokinesis. J Cell Biol 174: 485–490CrossrefCASPubMedWeb of Science®Google Scholar

Lipocortin III, ANXA3 tuottaa (hydrolysoi esiin) Inositoli-1-fosfaattimuotoa Ins-2-fosfaatista.

Reaktion merkitys:  Katabolinen  inositolipolyfosfaattien purkaminen fosfaateista  takaisin   siihen inositolimuotoon,  muotoon, josta  voi jälleen alkaa  fosfolipidien synteesi  ( kuten myoinositolin fosfatidihapon ja  CTP-energian avulla   de novo) solussa kohti  PI, PIP, PIP2 muotoja).

 https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/annexin

Inositol Phosphate Metabolism

Theodora S. Ross, in Cellular and Molecular Mechanisms of Inflammation: Signal Transduction in Inflammatory Cells, Part A, 1992

Cyclic Hydrolase

The primary sequence of the cyclic hydrolase is identical to that of lipocortin III, a member of a large family of homologous calcium- and phospholipid-binding proteins without defined biological functions (88). Some of these proteins have been shown to be phosphorylated in response to growth factors. The purified enzyme (33 kDa) is inhibited by inositol 2-phosphate [Ins(2)P], Zn²⁺, and glycerophosphoinositol (GroPIns) and stimulated by acidic phospholipids (87, 89). The pattern of interaction with particular phospholipids is the same as that previously observed for lipocortins (88, 90). The mechanism of inhibition by GroPIns is due to its ability to act as a substrate for this enzyme (89). The regulatory significance of this reaction is unclear, as the level of GroPIns-hydrolyzing activity measured in cellular extracts does not inversely correlate with the cellular levels of GroPIns (T. S. Ross and P. W. Majerus, unpublished observations). The presence of significant amounts of Ins(2)P and GroPIns in cells has been well documented (89, 91) and suggests that they may function as regulators of cellular cIns(1:2)P levels.

Measurement of the cyclic hydrolase activity in cellular extracts has unveiled a very interesting pattern. Cells with relatively low to nondetectable activity were either completely transformed or partially transformed (92). When levels of cyclic inositol phosphates were measured in these cells, it was found that cIns(1:2)P increased in proportion to the decreased cyclic hydrolase activity. The enzyme activity is also increased within one cell type when it is in a confluent state as compared to a logarithmically growing state. Overexpression of cyclic hydrolase in cells decreases the cIns(1:2)P levels as well as the final saturation density. In addition, high endogenous expression of cyclic hydrolase in cells tends to correlate with the differentiated state (e.g., high levels in platelets, brain, and neutrophils and low levels in several immortalized tissue culture cell lines of fibroblasts and T cells). The finding that this correlation exists both in nature and during heterologous expression of the enzyme makes the discovery of a cellular function for cIns(1:2)P likely to be successful. Further studies of the regulation of the cyclic hydrolase activity and cIns(1:2)P cellular levels will yield valuable information as to how to continue the quest for the function(s) of the cyclic bond.

 

 https://www.jlr.org/article/S0022-2275(20)34570-3/fulltext

 https://www.nature.com/articles/ncomms9505

 Jälkimmäisessä artikkelsisa näkyy se Ins-1 fosfaattimuoto, oka rikastuu  PIP muotoon eli muuttuu samalla  vesiliukoisten poly ja monofosfaattein  puolelta rasvaliukoisiin, fosfolipidien puolelle, jolloin siitä tulee  annexiinijärjestelmälle molekyyli, johon  jokin ANX  voi sitoutua. Ainakin ANXA2  tumankalvon  modifioinneissa  solunjaossa  sytokineesin alussa.  PI(4,5)P2 muoto on tuma-alueelle  tunnusomainen PL-muoto.  ( salvage tie, ei:  de novo tie)

ANGIOSTATIINI ja sen hyödylliset ominaisuudet. "Angiostatiini"-valmistettakin on.

 Normaalisti verisuonistossa kiertävästä Glu-plasminogeenistä  muodstuu - sen  havaittua hyytymää ja kiinnityttyä siihen suonen sisäpinnalla-  plasminogeeniä. Normaalisti kuitenkin muodostuu myös angiostatiinia 3%:sti plasminogeenistä.  Onpohdittu, miten  se muodostuu.

tiedetään ainkin, että matrixmetalloproteiineista käsin- niiden aktivoiduttua plasmiinista  preMMP-muodosta MMP-muotoon, usea MMP pystyy pilkkomaan Glu-PLG- muodsta angiotensiinia esiin.  Näistä on mainittu elastaasi tässä alla olevassa linkissä. Elastaasi voi tuottaa kahta eri kokoa angiostatiinia: toisessa on  4 rinkulaa jäljellä ja toisessa vain 3 rinkulaa,   niitä rinkuloita , joita plasminogeenillä ja plasmiinilla on 5 kpl. 

Ainakin lyhemmällä angiostatiinilla on havaittu aivan tuumorin kasvua  vastustavaa vaikutusta.  Suoniston sisällä  hyytymässä alkavaa neovaskularisaatiotaipumusta  tietysti vastustaa heti jo angiostatiinin  pitempikin muoto.  tuumorfeista on identifioitu angiostatiinin kaltainen molekyyli, joka oli hieman päistään lyhempi kuin normaalit angiostatiinimuodot.  Lääketehdas taas on kehittänyt  angiostatiinimuodon, joka kattaa angiostatiinin molempien päiden rakenteet ja on tehty verisuoistossa kiertävästä  plasminogeenistä. Sillä on todettu eläinkokeissa antiproleratiivista vaikutusta, tosin sen käyttäminen tai testaaminen lääkkeenä ei ole helppoa,sillä rakenneta täytyy säilyttää  alle 70 celsiusasteen pakkasessa. 

https://www.haemtech.com/products/protease-inhibitors/human-angiostatin

 

 

Perustava molekyyli PLASMINOGEENI (PLG) omaa kaksi glykoformia ihmisessä Tyyppi I ja Tyyppi II

 https://diapharma.com/plasminogen-plg/

Sitaatti 18.10.2022: 

"Plasminogen (PLG)

Plasmin is released as a zymogen called plasminogen (PLG) from the liver into the factor IX systemic circulation. Two major glycoforms of plasminogen are present in humans – type I plasminogen contains two glycosylation moieties (N-linked to N289 and O-linked to T346), whereas type II plasminogen contains only a single O-linked sugar (O-linked to T346). Type II plasminogen is preferentially recruited to the cell surface over the type I glycoform. Conversely, type I plasminogen appears more readily recruited to blood clots."

(Tässä lähteessä kaavat Plasminogeeni, sen aktivaattorit   t-PA kudosaktivaattori ja  munuaisperäinen u-PA) .

 

 

Pseudogeeni 19q13.42 Diphosphoinositol polyphosphate phosphohydrolase ja sen funktion tekeviä geenejä

 Tämän kaltaista   funktiota on usealla  fosfohydrolaasilla, mutta  tälle geenille ei löytynyt paikan lisäksi muuta erityistietoa. (Tällä ryhmällä 

		NUDT3	Nudix Hydrolase 3	Protein Coding	38	GC06M069334	38.75
2		NUDT4	Nudix Hydrolase 4	Protein Coding	40	GC12P093412	37.54
3		NUDT11	Nudix Hydrolase 11	Protein Coding	37	GC0XM051490	36.56
4		NUDT10	Nudix Hydrolase 10	Protein Coding	35	GC0XP051332	33.10
5		ENSG00000267689	Diphosphoinositol Polyphosphate Phosphohydrolase 2, Pseudogene

GeneCards Summary for ENSG00000267689 Gene

ENSG00000267689 (Diphosphoinositol Polyphosphate Phosphohydrolase 2, Pseudogene) is a Pseudogene.

Additional gene information for ENSG00000267689 Gene

• Ensembl (ENSG00000267689)
• 
  
  

IMPA, Inositolimonofosfataasi 1 (8q21.13)

 https://alphafold.ebi.ac.uk/entry/P29218

Protein

Inositol monophosphatase 1

Gene

IMPA1

Source organism

Homo sapiens (Human)go to search

UniProt

P29218go to UniProt

Experimental structures

13 structures in PDB for P29218go to PDBe-KB

Biological function

Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates.go to UniProt

• GeneCards Symbol: IMPA1 ²
• Inositol Monophosphatase 1 ^{2 3 4 5}
• IMPA ^{3 4 5}
• Lithium-Sensitive Myo-Inositol Monophosphatase A1 ^{3 4}
• Inositol(Myo)-1(Or 4)-Monophosphatase 1 ^{2 3}
• D-Galactose 1-Phosphate Phosphatase ^{3 4}
• Inositol-1(Or 4)-Monophosphatase 1 ^{3 4}
• Myo-Inositol Monophosphatase 1 ^{2 3}

• EC 3.1.3.25 ^{4 48}
• IMPase 1 ^{3 4}
• IMP 1 ^{3 4}
• Testicular Tissue Protein Li 94 ³
• EC 3.1.3.94 ⁴
• MRT59 ³
• IMP ³

External Ids for IMPA1 Gene

 

Annexiini A3, ANXA3 , pilkkoo syklisestä inositoli-1,2-fosfaatista esiin ins(1)fosfaattia

 

( 4q21.21) ANXA3 , Annexin A3

(inositoli-1,2- cykl.fosfaatti-2 fosfohydrolaasi)

https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P12429

ANXA3

Organism:

Homo sapiens (Human)

Synonyms:

ANX3

Uniprot:

P12429go to UniProt

Biological function:

Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate go to UniProt

Aliases for ANXA3 Gene

https://www.genecards.org/cgi-bin/carddisp.plgene=ANXA3&keywords=ANXA3

• GeneCards Symbol: ANXA3

• Annexin A3

• ANX3

• Inositol 1,2-Cyclic Phosphate 2-Phosphohydrolase

• Placental Anticoagulant Protein III

• 35-Alpha Calcimedin

• Lipocortin III

• Annexin-3

• PAP-III

• Annexin III (Lipocortin III, 1,2-Cyclic-Inositol-Phosphate Phosphodiesterase, Placental Anticoagulant Protein III, Calcimedin 35-Alpha)

• Annexin III (Lipocortin III)

• Calcimedin 35-Alpha

• Annexin III

External Ids for ANXA3 Gene

Entrez Gene Summary for ANXA3 GeneThis gene encodes a member of the annexin family. Members of this calcium-dependent phospholipid-binding protein family play a role in the regulation of cellular growth and in signal transduction pathways. This protein functions in the inhibition of phopholipase A2 and cleavage of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. This protein may also play a role in anti-coagulation. [provided by RefSeq, Jul 2008]

GeneCards Summary for ANXA3 Gene

ANXA3 (Annexin A3) is a Protein Coding gene. Diseases associated with ANXA3 include Ovarian Cancer and Prostate Cancer. Among its related pathways are Prostaglandin synthesis and regulation. Gene Ontology (GO) annotations related to this gene include calcium ion binding and calcium-dependent phospholipid binding. An important paralog of this gene is ANXA4.

UniProtKB/Swiss-Prot Summary for ANXA3 Gene

Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. ( ANXA3_HUMAN,P12429 )

Inositolipolyfosfaattien metaboliasta Avustusta HCV ja SARS-2 koronaviruksen viruksen replikaatio-organellin luomiseen.

 

https://pubmed.ncbi.nlm.nih.gov/27701417/

https://pubmed.ncbi.nlm.nih.gov/23107997/

https://pubmed.ncbi.nlm.nih.gov/24152294

The enzymes of human diphosphoinositol polyphosphate metabolism

https://pubmed.ncbi.nlm.nih.gov/10777568/

. 2000 Apr 28;275(17):12730-6.

doi: 10.1074/jbc.275.17.12730.

Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family

 

https://www.pnas.org/doi/full/10.1073/pnas.1922284117 

InsP₇ is a small-molecule regulator of NUDT3-mediated mRNA decapping and processing-body dynamics

 Article| Volume 37, ISSUE 8, 110049, November 23, 2021:

• PDF
• Figures
•  Contribution of autophagy machinery factors to HCV and SARS-CoV-2 replication organelle formation

• Woan-Ing Twu

Open AccessPublished:November 09, 2021DOI:https://doi.org/10.1016/j.celrep.2021.110049

 

(Kommentti: Artikkeli mainitsee proteiinifosfataasin, jolla on FYVEdomeeni,  ZFYVE1 alias   tekijän  DFCP1 , joka osallistuu  viruksen  replikaatio-organellin (Double Membrane vesicles) tekoon.   Tässä on apuna Class III PI3K kompleksi ja sen tuote PI3P-lipidi.

Toisesta lähteestä (2020 )   on tieto, että  Sars-Cov-2 nsp 13 rekrytoi  myös ZFYVE7. Se on toiselta nimeltä  FYCO1. 

 

Artikkeli ennen Sars-2 aikaa vuodelta 2010 FYCo1 funktiosta :   https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2812517/  

 

 Autophagy is the main eukaryotic degradation pathway for long-lived proteins, protein aggregates, and cytosolic organelles. Although the protein machinery involved in the biogenesis of autophagic vesicles is well described, very little is known about the mechanism of cytosolic transport of autophagosomes. In this study, we have identified an adaptor protein complex, formed by the two autophagic membrane-associated proteins LC3 and Rab7 and the novel FYVE and coiled-coil (CC) domain–containing protein FYCO1, that promotes microtubule (MT) plus end–directed transport of autophagic vesicles. We have characterized the LC3-, Rab7-, and phosphatidylinositol-3-phosphate–binding domains in FYCO1 and mapped part of the CC region essential for MT plus end–directed transport. We also propose a mechanism for selective autophagosomal membrane recruitment of FYCO1.   

 

(Huom: Virukset HCV ja Sars-cov2 eivät kuitenkaan johda autofagiakompleksin tekoon, vaan  fagoforivaiheesta  sulkeutuvaan kaksoisrakkulaan (DMV), joka on replikaatio-organelli näille viruksille).