PMID- 10226031
OWN - NLM
STAT- MEDLINE
DCOM- 19990601
LR  - 20190728
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 9
IP  - 8
DP  - 1999 Apr 22
TI  - The APC-associated protein EB1 associates with components of the dynactin complex
      and cytoplasmic dynein intermediate chain.
PG  - 425-8
AB  - Human EB1 is a highly conserved protein that binds to the carboxyl terminus of
      the human adenomatous polyposis coli (APC) tumor suppressor protein [1], a domain
      of APC that is commonly deleted in colorectal neoplasia [2]. EB1 belongs to a
      family of microtubule-associated proteins that includes Schizosaccharomyces pombe
      Mal3 [3] and Saccharomyces cerevisiae Bim1p [4]. Bim1p appears to regulate the
      timing of cytokinesis as demonstrated by a genetic interaction with Act5, a
      component of the yeast dynactin complex [5]. Whereas the predominant function of 
      the dynactin complex in yeast appears to be in positioning the mitotic spindle
      [6], in animal cells, dynactin has been shown to function in diverse processes,
      including organelle transport, formation of the mitotic spindle, and perhaps
      cytokinesis [7] [8] [9] [10]. Here, we demonstrate that human EB1 can be
      coprecipitated with p150(Glued), a member of the dynactin protein complex. EB1
      was also found associated with the intermediate chain of cytoplasmic dynein
      (CDIC) and with dynamitin (p50), another component of the dynactin complex, but
      not with dynein heavy chain, in a complex that sedimented at approximately 5S in 
      a sucrose density gradient. The association of EB1 with members of the dynactin
      complex was independent of APC and was preserved in the absence of an intact
      microtubule cytoskeleton. The molecular interaction of EB1 with members of the
      dynactin complex and with CDIC may be important for microtubule-based processes.
FAU - Berrueta, L
AU  - Berrueta L
AD  - Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical
      School, Boston, Massachussetts 02115, USA.
FAU - Tirnauer, J S
AU  - Tirnauer JS
FAU - Schuyler, S C
AU  - Schuyler SC
FAU - Pellman, D
AU  - Pellman D
FAU - Bierer, B E
AU  - Bierer BE
LA  - eng
PT  - Journal Article
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Adenomatous Polyposis Coli Protein)
RN  - 0 (CTNNB1 protein, human)
RN  - 0 (Cell Extracts)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (DCTN1 protein, human)
RN  - 0 (DCTN2 protein, human)
RN  - 0 (Dynactin Complex)
RN  - 0 (EP1 protein, Daucus carota)
RN  - 0 (Glycoproteins)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (NIP100 protein, S cerevisiae)
RN  - 0 (Plant Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (beta Catenin)
RN  - EC 3.6.4.2 (Dyneins)
SB  - IM
MH  - Adenomatous Polyposis Coli Protein
MH  - Animals
MH  - CHO Cells
MH  - Cell Extracts/chemistry
MH  - Cricetinae
MH  - Cytoplasm/chemistry
MH  - Cytoskeletal Proteins/*metabolism
MH  - Dynactin Complex
MH  - Dyneins/chemistry/*metabolism
MH  - Glycoproteins/*metabolism
MH  - Humans
MH  - Jurkat Cells
MH  - Microtubule-Associated Proteins/*metabolism
MH  - Microtubules/metabolism
MH  - Plant Proteins/*metabolism
MH  - Precipitin Tests
MH  - Saccharomyces cerevisiae Proteins
MH  - *Trans-Activators
MH  - Tumor Cells, Cultured
MH  - beta Catenin
EDAT- 1999/05/05 00:00
MHDA- 1999/05/05 00:01
CRDT- 1999/05/05 00:00
PHST- 1999/05/05 00:00 [pubmed]
PHST- 1999/05/05 00:01 [medline]
PHST- 1999/05/05 00:00 [entrez]
AID - S0960-9822(99)80190-0 [pii]
AID - 10.1016/s0960-9822(99)80190-0 [doi]
PST - ppublish
SO  - Curr Biol. 1999 Apr 22;9(8):425-8. doi: 10.1016/s0960-9822(99)80190-0.