PMID- 10488091
OWN - NLM
STAT- MEDLINE
DCOM- 19991104
LR  - 20191210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 39
DP  - 1999 Sep 24
TI  - The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and initial
      characterization.
PG  - 27553-61
AB  - ARF-like proteins (ARLs) comprise a functionally distinct group of incompletely
      characterized members in the ARF family of RAS-related GTPases. We took advantage
      of the GTP binding characteristics of human ARL2 to develop a specific, high
      affinity binding assay that allowed the purification of a novel ARL2-binding
      protein. A 19-kDa protein (BART, Binder of Arl Two) was identified and purified
      from bovine brain homogenate. BART binding is specific to ARL2.GTP with high
      affinity but does not interact with ARL2.GDP or activated ARF or RHO proteins.
      Based on peptide sequences of purified bovine BART, the human cDNA sequence was
      determined. The 489-base pair BART open reading frame encodes a novel 163-amino
      acid protein with a predicted molecular mass of 18,822 Da. Recombinant BART was
      found to bind ARL2.GTP in a manner indistinguishable from native BART. Northern
      and Western analyses indicated BART is expressed in all tissues sampled. The lack
      of detectable membrane association of ARL2 or BART upon activation of ARL2 is
      suggestive of actions quite distinct from those of the ARFs. The lack of ARL2
      GTPase-activating protein activity in BART led us to conclude that the specific
      interaction with ARL2.GTP is most consistent with BART being the first identified
      ARL2-specific effector.
FAU - Sharer, J D
AU  - Sharer JD
AD  - Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia
      30322-3050, USA.
FAU - Kahn, R A
AU  - Kahn RA
LA  - eng
SI  - GENBANK/AF126062
GR  - 1F32CA73202/CA/NCI NIH HHS/United States
GR  - R01GM55148/GM/NIGMS NIH HHS/United States
GR  - R01GM55823/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (ARL2BP protein, human)
RN  - 0 (Arl2bp protein, mouse)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Membrane Transport Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Recombinant Proteins)
RN  - 146-91-8 (Guanosine Diphosphate)
RN  - 34273-04-6 (Guanylyl Imidodiphosphate)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Carrier Proteins/*genetics/isolation & purification/*metabolism
MH  - Cattle
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics
MH  - GTP Phosphohydrolases/*metabolism
MH  - GTP-Binding Proteins/*metabolism
MH  - Guanosine Diphosphate/metabolism
MH  - Guanosine Triphosphate/metabolism
MH  - Guanylyl Imidodiphosphate/metabolism
MH  - Humans
MH  - Kinetics
MH  - Membrane Transport Proteins
MH  - Mice
MH  - Molecular Sequence Data
MH  - Open Reading Frames
MH  - Peptide Fragments/chemistry
MH  - Recombinant Proteins/isolation & purification/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
EDAT- 1999/09/17 00:00
MHDA- 1999/09/17 00:01
CRDT- 1999/09/17 00:00
PHST- 1999/09/17 00:00 [pubmed]
PHST- 1999/09/17 00:01 [medline]
PHST- 1999/09/17 00:00 [entrez]
AID - 10.1074/jbc.274.39.27553 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 24;274(39):27553-61. doi: 10.1074/jbc.274.39.27553.