PMID- 10189370
OWN - NLM
STAT- MEDLINE
DCOM- 19990506
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 145
IP  - 1
DP  - 1999 Apr 5
TI  - GMAP-210, A cis-Golgi network-associated protein, is a minus end
      microtubule-binding protein.
PG  - 83-98
AB  - We report that a peripheral Golgi protein with a molecular mass of 210 kD
      localized at the cis-Golgi network (Rios, R.M., A.M. Tassin, C. Celati, C.
      Antony, M.C. Boissier, J.C. Homberg, and M. Bornens. 1994. J. Cell Biol.
      125:997-1013) is a microtubule-binding protein that associates in situ with a
      subpopulation of stable microtubules. Interaction of this protein, now called
      GMAP-210, for Golgi microtubule-associated protein 210, with microtubules in
      vitro is direct, tight and nucleotide-independent. Biochemical analysis further
      suggests that GMAP-210 specifically binds to microtubule ends. The full-length
      cDNA encoding GMAP-210 predicts a protein of 1, 979 amino acids with a very long 
      central coiled-coil domain. Deletion analyses in vitro show that the COOH
      terminus of GMAP-210 binds to microtubules whereas the NH2 terminus binds to
      Golgi membranes. Overexpression of GMAP-210-encoding cDNA induced a dramatic
      enlargement of the Golgi apparatus and perturbations in the microtubule network. 
      These effects did not occur when a mutant lacking the COOH-terminal domain was
      expressed. When transfected in fusion with the green fluorescent protein, the
      NH2-terminal domain associated with the cis-Golgi network whereas the
      COOH-terminal microtubule-binding domain localized at the centrosome. Altogether 
      these data support the view that GMAP-210 serves to link the cis-Golgi network to
      the minus ends of centrosome-nucleated microtubules. In addition, this
      interaction appears essential for ensuring the proper morphology and size of the 
      Golgi apparatus.
FAU - Infante, C
AU  - Infante C
AD  - Departamento de Microbiologia, Facultad de Biologia, Universidad de Sevilla Apdo.
      1095, 41080-Sevilla, Spain.
FAU - Ramos-Morales, F
AU  - Ramos-Morales F
FAU - Fedriani, C
AU  - Fedriani C
FAU - Bornens, M
AU  - Bornens M
FAU - Rios, R M
AU  - Rios RM
LA  - eng
SI  - GENBANK/Y12490
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (DNA, Complementary)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (Molecular Motor Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (TRIP11 protein, human)
RN  - 0 (Tubulin)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - P88XT4IS4D (Paclitaxel)
SB  - IM
EIN - J Cell Biol 2002 Aug 5;158(3):593
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - COS Cells
MH  - Centrosome/*metabolism
MH  - DNA, Complementary/genetics
MH  - Genes, Reporter
MH  - Golgi Apparatus/*metabolism/ultrastructure
MH  - Green Fluorescent Proteins
MH  - HeLa Cells
MH  - Humans
MH  - Interphase
MH  - Luminescent Proteins/analysis/genetics
MH  - Microscopy, Fluorescence
MH  - Microtubule-Associated Proteins/genetics/*isolation & purification/physiology
MH  - Microtubules/*metabolism
MH  - Molecular Motor Proteins
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Nuclear Proteins
MH  - Paclitaxel/metabolism/pharmacology
MH  - Recombinant Fusion Proteins/metabolism
MH  - Sequence Deletion
MH  - Transfection
MH  - Tubulin/metabolism
PMC - PMC2148210
EDAT- 1999/04/06 00:00
MHDA- 1999/04/06 00:01
CRDT- 1999/04/06 00:00
PHST- 1999/04/06 00:00 [pubmed]
PHST- 1999/04/06 00:01 [medline]
PHST- 1999/04/06 00:00 [entrez]
AID - 10.1083/jcb.145.1.83 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Apr 5;145(1):83-98. doi: 10.1083/jcb.145.1.83.