Literature DB >> 1570018

Actin-dependent organelle movement in squid axoplasm.

S A Kuznetsov1, G M Langford, D G Weiss.   

Abstract

Studies of organelle movement in axoplasm extruded from the squid giant axon have led to the basic discoveries of microtubule-dependent organelle motility and the characterization of the microtubule-based motor proteins kinesin and cytoplasmic dynein. Rapid organelle movement in higher animal cells, especially in neurons, is considered to be microtubule-based. The role of actin filaments, which are also abundant in axonal cytoplasm, has remained unclear. The inhibition of organelle movement in axoplasm by actin-binding proteins such as DNase I, gelsolin and synapsin I has been attributed to their ability to disorganize the microtubule domains where most of the actin-filaments are located. Here we provide evidence of a new type of organelle movement in squid axoplasm which is independent of both microtubules and microtubule-based motors. This movement is ATP-dependent, unidirectional, actin-dependent, and probably generated by a myosin-like motor. These results demonstrate that an actomyosin-like mechanism can be directly involved in the generation of rapid organelle transport in nerve cells.

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Year:  1992        PMID: 1570018     DOI: 10.1038/356722a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  110 in total

1.  Association of actin filaments with axonal microtubule tracts.

Authors:  E L Bearer; T S Reese
Journal:  J Neurocytol       Date:  1999-02

2.  Squid axoplasm supports the retrograde axonal transport of herpes simplex virus.

Authors:  E L Bearer; M L Schlief; X O Breakefield; D E Schuback; T S Reese; J H LaVail
Journal:  Biol Bull       Date:  1999-10       Impact factor: 1.818

3.  Models of motor-assisted transport of intracellular particles.

Authors:  D A Smith; R M Simmons
Journal:  Biophys J       Date:  2001-01       Impact factor: 4.033

4.  Retrograde axonal transport of herpes simplex virus: evidence for a single mechanism and a role for tegument.

Authors:  E L Bearer; X O Breakefield; D Schuback; T S Reese; J H LaVail
Journal:  Proc Natl Acad Sci U S A       Date:  2000-07-05       Impact factor: 11.205

5.  Association of a nonmuscle myosin II with axoplasmic organelles.

Authors:  Joseph A DeGiorgis; Thomas S Reese; Elaine L Bearer
Journal:  Mol Biol Cell       Date:  2002-03       Impact factor: 4.138

6.  Dynamics of immature secretory granules: role of cytoskeletal elements during transport, cortical restriction, and F-actin-dependent tethering.

Authors:  R Rudolf; T Salm; A Rustom; H H Gerdes
Journal:  Mol Biol Cell       Date:  2001-05       Impact factor: 4.138

7.  Microtubule-independent motility and nuclear targeting of adenoviruses with fluorescently labeled genomes.

Authors:  J B Glotzer; A I Michou; A Baker; M Saltik; M Cotten
Journal:  J Virol       Date:  2001-03       Impact factor: 5.103

8.  ATP-dependent membrane assembly of F-actin facilitates membrane fusion.

Authors:  A Jahraus; M Egeberg; B Hinner; A Habermann; E Sackman; A Pralle; H Faulstich; V Rybin; H Defacque; G Griffiths
Journal:  Mol Biol Cell       Date:  2001-01       Impact factor: 4.138

9.  PLAC-24 is a cytoplasmic dynein-binding protein that is recruited to sites of cell-cell contact.

Authors:  Sher Karki; Lee A Ligon; Jamison DeSantis; Mariko Tokito; Erika L F Holzbaur
Journal:  Mol Biol Cell       Date:  2002-05       Impact factor: 4.138

10.  The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1).

Authors:  C M Waterman-Storer; S Karki; E L Holzbaur
Journal:  Proc Natl Acad Sci U S A       Date:  1995-02-28       Impact factor: 11.205

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