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04 Vesicle Transport

Coat selfassembly drives membrane curvature. Dynamin hydrolysis is required for pinching off of clathrin-coated vesicles. Vesicle fusion requires SNARE combinatorics.

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70 views35 pages

04 Vesicle Transport

Coat selfassembly drives membrane curvature. Dynamin hydrolysis is required for pinching off of clathrin-coated vesicles. Vesicle fusion requires SNARE combinatorics.

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Anonymous vhjGsvp
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VesicleTransport

VesicleFormation
Curvature(SelfAssemblyofCoatcomplex)
Sorting(SortingComplexformation)
Regulation(Sar1/Arf1GTPases)
Fission(constrictases)
MembraneFusion
Fusases
SNAREcombinatorics
Tethers
RegulationbyRabs
SMProteins

Secretorypathway:manycompartments,
interconnectedbytraffickingroutes

TwoKeySteps:
1.sortingduringvesicleformation
2.targetingduringvesiclefusion

MorphologicalExperiments
SuggestRoleofVesicleCoats

Eachtypeactsatdistinctlocations

Components that participate in budding


of coated vesicles

Figure 17-51

Sar1GEFcontrolssiteofCOPIIrecruitment

CoatcomponentshaveassociatedGAP:
uncoatingand/orsorting?

CargobindingsitesonCOPIISec24

QuickTime and aTIFF (LZW) decompressorare needed to see this picture.

Arg=Sec22
B=Diacidic,
Bet1

A=Sed5

Notealso:bindsSNAREafterbutnotbeforeactivation

Ligandcontrolof
sortingcomplex
formation

TakeHome:Coatselfassemblydrives
membranecurvature.Howwasthis
determined,howdoesitwork?

ClathrinAssemblyMovie

QuickTime and a
Sorenson Video 3 decompressor
are needed to see this picture.

Inductionofcurvaturealsoinvolvescoatcomplex
membraneattachment(&penetration

Cell,Vol.111,143146,October18,2002,Copyrighto2002byCellPress

MinireviewEndocytosis:DrivingMembranes
aroundtheBend

JamesH.Hurley1,3andBeverlyWendland2,3

MembranePenetrationbyEpsin
Insideoutamphipathichelixinserts
uponinteractionw/PIP2
therebydisplacinglipidheadgroups.
Thismaycauserotationofacyltails
(egthephosphatidylcholineshown)
intothevacatedspace.

Epsin

DynaminAssemblesatNeck

GTP hydrolysis by dynamin is required


for pinching off of clathrin-coated vesicles

Figure 17-55

ERGIC/VTCmovesalongmicrotubules

DockingSpecifiesFusionSite

Hydration
barrierto
spontaneous
fusion

SNAREsform4strandedcoiledcoilcorecomplex

Q&RSNAREsubunits

ToxinsSpecificallyCleaveSNAREs

Trimerofhairpins:C
peptidesareeffective
dominantneg.inhibs

Cis Core complex reversed by NSF/SNAPs

trans

cis

Secretorypathway:manycompartments,
interconnectedbytraffickingroutes

LiveImagingofVSVGGFPTransport

QuickTime and a
Sorenson Video 3 decompressor
are needed to see this picture.

The Golgi is the central processing and sorting station of the


secretory pathway

ER

ERGIC
Golgi

ER

ERGIC

Golgi

HomotypicfusionCOPIIvesiclesmayformERGIC/VTCs

VTCmorphology

ERGIC/VTCmovesalongmicrotubules

The Golgi maintains its complex structure in the presence of


continuous membrane traffic

trans
medial
cis

Evidenceforenzymecompartmentalization

3DViewofGolgiStack

Vesicle&MaturationModels

TwoKeySteps:sortingduring
vesicleformation&targetingduring
vesiclefusion

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