PMID- 10607597
OWN - NLM
STAT- MEDLINE
DCOM- 20000216
LR  - 20190728
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 9
IP  - 24
DP  - 1999 Dec 16-30
TI  - Interaction of the p62 subunit of dynactin with Arp1 and the cortical actin
      cytoskeleton.
PG  - 1497-500
AB  - Targeting of the minus-end directed microtubule motor cytoplasmic dynein to a
      wide array of intracellular substrates appears to be mediated by an accessory
      factor known as dynactin [1-4]. Dynactin is a multi-subunit complex that contains
      a short actin-related protein 1 (Arp 1) filament with capZ at the barbed end and 
      p62 at the pointed end [5]. The location of the p62 subunit and the proposed role
      for dynactin as a multifunctional targeting complex raise the possibility of a
      dual role for p62 in dynein targeting and in Arp1 pointed-end capping. In order
      to gain further insight into the role of p62 in dynactin function, we have cloned
      cDNAs that encode two full-length isoforms of the protein from rat brain. We
      found that p62 is homologous to the nuclear migration protein Ropy-2 from
      Neurospora [6]; both proteins contain a zinc-binding motif that resembles the LIM
      domain of several other cytoskeletal proteins [7]. Overexpression of p62 in
      cultured mammalian cells revealed colocalization with cortical actin, stress
      fibers, and focal adhesion sites, sites of potential interaction between
      microtubules and the cell cortex [8,9]. The p62 protein also colocalized with
      polymers of overexpressed wild-type or barbed-end-mutant Arp1, but not with a
      pointed-end mutant. Deletion of the LIM domain abolished targeting of p62 to
      focal-adhesion sites but did not interfere with binding of p62 to actin or Arp1. 
      These data implicate p62 in Arp1 pointed-end binding and suggest additional roles
      in linking dynein and dynactin to the cortical cytoskeleton.
FAU - Garces, J A
AU  - Garces JA
AD  - Department of Cell Biology, University of Massachusetts Medical School, Worcester
      01605, USA.
FAU - Clark, I B
AU  - Clark IB
FAU - Meyer, D I
AU  - Meyer DI
FAU - Vallee, R B
AU  - Vallee RB
LA  - eng
SI  - GENBANK/AF192493
SI  - GENBANK/AF192494
PT  - Journal Article
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Actins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Dbnl protein, rat)
RN  - 0 (Dynactin Complex)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (Protein Isoforms)
RN  - 0 (Recombinant Proteins)
RN  - 0 (actin-related protein 1, rat)
SB  - IM
MH  - Actins/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - COS Cells
MH  - Cloning, Molecular
MH  - Cytoskeleton/*metabolism
MH  - DNA, Complementary/genetics
MH  - Dynactin Complex
MH  - *Microfilament Proteins
MH  - Microtubule-Associated Proteins/*chemistry/genetics/*metabolism
MH  - Models, Molecular
MH  - Mutation
MH  - Protein Isoforms/chemistry/genetics/metabolism
MH  - Protein Structure, Quaternary
MH  - Rats
MH  - Recombinant Proteins/chemistry/genetics/metabolism
MH  - Sequence Deletion
MH  - Zinc Fingers/genetics
MH  - *src Homology Domains
EDAT- 1999/12/23 09:00
MHDA- 2000/02/19 09:00
CRDT- 1999/12/23 09:00
PHST- 1999/12/23 09:00 [pubmed]
PHST- 2000/02/19 09:00 [medline]
PHST- 1999/12/23 09:00 [entrez]
AID - S0960-9822(00)80122-0 [pii]
AID - 10.1016/s0960-9822(00)80122-0 [doi]
PST - ppublish
SO  - Curr Biol. 1999 Dec 16-30;9(24):1497-500. doi: 10.1016/s0960-9822(00)80122-0.