PMID- 10336464
OWN - NLM
STAT- MEDLINE
DCOM- 19990629
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 22
DP  - 1999 May 28
TI  - Splice variants of intersectin are components of the endocytic machinery in
      neurons and nonneuronal cells.
PG  - 15671-7
AB  - We recently identified and cloned intersectin, a protein containing two Eps15
      homology (EH) domains and five Src homology 3 (SH3) domains. Using a newly
      developed intersectin antibody, we demonstrate that endogenous COS-7 cell
      intersectin localizes to clathrin-coated pits, and transfection studies suggest
      that the EH domains may direct this localization. Through alternative splicing in
      a stop codon, a long form of intersectin is generated with a C-terminal extension
      containing Dbl homology (DH), pleckstrin homology (PH), and C2 domains. Western
      blots reveal that the long form of intersectin is expressed specifically in
      neurons, whereas the short isoform is expressed at lower levels in glia and other
      nonneuronal cells. Immunofluorescence analysis of cultured hippocampal neurons
      reveals that intersectin is found at the plasma membrane where it is co-localized
      with clathrin. Ibp2, a protein identified based on its interactions with the EH
      domains of intersectin, binds to clathrin through the N terminus of the heavy
      chain, suggesting a mechanism for the localization of intersectin at
      clathrin-coated pits. Ibp2 also binds to the clathrin adaptor AP2, and antibodies
      against intersectin co-immunoprecipitate clathrin, AP2, and dynamin from brain
      extracts. These data suggest that the long and short forms of intersectin are
      components of the endocytic machinery in neurons and nonneuronal cells.
FAU - Hussain, N K
AU  - Hussain NK
AD  - Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill
      University, Montreal, QC, H3A 2B4, Canada.
FAU - Yamabhai, M
AU  - Yamabhai M
FAU - Ramjaun, A R
AU  - Ramjaun AR
FAU - Guy, A M
AU  - Guy AM
FAU - Baranes, D
AU  - Baranes D
FAU - O'Bryan, J P
AU  - O'Bryan JP
FAU - Der, C J
AU  - Der CJ
FAU - Kay, B K
AU  - Kay BK
FAU - McPherson, P S
AU  - McPherson PS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Protein Complex 2)
RN  - 0 (Adaptor Protein Complex alpha Subunits)
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Carrier Proteins)
RN  - 0 (Clathrin)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (IBP2 protein, Zea mays)
RN  - 0 (Membrane Proteins)
RN  - 0 (Plant Proteins)
RN  - 0 (intersectin 1)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.5.5 (Dynamins)
SB  - IM
MH  - Adaptor Protein Complex 2
MH  - Adaptor Protein Complex alpha Subunits
MH  - Adaptor Proteins, Vesicular Transport
MH  - Alternative Splicing
MH  - Animals
MH  - COS Cells
MH  - Carrier Proteins/*genetics
MH  - Cell Membrane/metabolism
MH  - Clathrin/metabolism
MH  - Cloning, Molecular
MH  - Coated Pits, Cell-Membrane/metabolism
MH  - DNA-Binding Proteins/metabolism
MH  - Dynamins
MH  - Endocytosis/*genetics
MH  - GTP Phosphohydrolases/metabolism
MH  - Gene Expression
MH  - Hippocampus/metabolism
MH  - Membrane Proteins
MH  - Neurons/*metabolism
MH  - *Plant Proteins
MH  - Rats
MH  - Xenopus laevis
MH  - src Homology Domains/genetics
EDAT- 1999/05/21 00:00
MHDA- 1999/05/21 00:01
CRDT- 1999/05/21 00:00
PHST- 1999/05/21 00:00 [pubmed]
PHST- 1999/05/21 00:01 [medline]
PHST- 1999/05/21 00:00 [entrez]
AID - 10.1074/jbc.274.22.15671 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 May 28;274(22):15671-7. doi: 10.1074/jbc.274.22.15671.