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BibTeX
Membrane associated nonmuscle myosin II functions as a motor for actin-based vesicle transport in clam oocyte extracts
Cell motility and the cytoskeleton, 2007-10, Vol.64 (10), p.739-755
DePina, Ana S.
Wöllert, Torsten
Langford, George M.
2007
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
DePina, Ana S.
Wöllert, Torsten
Langford, George M.
Titel
Membrane associated nonmuscle myosin II functions as a motor for actin-based vesicle transport in clam oocyte extracts
Ist Teil von
Cell motility and the cytoskeleton, 2007-10, Vol.64 (10), p.739-755
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2007
Quelle
Wiley-Blackwell Journals
Beschreibungen/Notizen
Nonmuscle myosin II (Myo2) has been shown to associate with membranes of the trans‐Golgi network and to be involved in Golgi to ER retrograde protein transport. Here, we provide evidence that Myo2 not only associates with membranes but functions to transport vesicles on actin filaments (AFs). We used extracts from unactivated clam oocytes for these studies. AFs assembled spontaneously in these extracts and myosin‐dependent vesicle transport was observed upon activation. In addition, actin bundles formed and moved relative to each other at an average speed of ˜0.30 μm/s. Motion analysis revealed that vesicles moved on the spontaneously assembled AFs at speeds greater than 1 μm/s. The motor on these vesicles was identified as a member of the nonmuscle Myo2 family based on sequence determination by Edman chemistry. Vesicles in these extracts were purified by sucrose gradient centrifugation and movement was reconstituted in vitro using skeletal muscle actin coated coverslips. When peripheral membrane proteins of vesicles including Myo2 were removed by salt stripping or when extracts were treated with an antibody specific to clam oocyte nonmuscle Myo2, vesicle movement was inhibited. Blebbistatin, a Myo2 specific inhibitor, also blocked vesicle movement. Myo2 light chain kinase activity was found to be essential for vesicle movement and sliding of actin bundles. Together, our data provide direct evidence that nonmuscle Myo2 is involved in actin‐dependent vesicle transport in clam oocytes. Cell Motil. Cytoskeleton 2007. © 2007 Wiley‐Liss, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 0886-1544
eISSN: 1097-0169
DOI: 10.1002/cm.20219
Titel-ID: cdi_crossref_primary_10_1002_cm_20219
Format
–
Schlagworte
Actins - metabolism
,
Amino Acid Sequence
,
Animals
,
Biological Transport
,
blebbistatin
,
cytoskeleton
,
Cytoskeleton - metabolism
,
Heterocyclic Compounds, 4 or More Rings - adverse effects
,
membrane transport
,
molecular motors
,
Molecular Sequence Data
,
motility
,
Myosin Type II - antagonists & inhibitors
,
Myosin Type II - chemistry
,
Myosin Type II - metabolism
,
Oocytes - chemistry
,
Oocytes - metabolism
,
Secretory Vesicles - metabolism
,
Sequence Homology, Amino Acid
,
Spisula - metabolism
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