PMID- 10542231
OWN - NLM
STAT- MEDLINE
DCOM- 19991213
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 45
DP  - 1999 Nov 5
TI  - The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of 
      synaptojanin 1 at distinct sites that display an unconventional binding
      specificity.
PG  - 32001-7
AB  - The proline-rich domain of synaptojanin 1, a synaptic protein with
      phosphatidylinositol phosphatase activity, binds to amphiphysin and to a family
      of recently discovered proteins known as the SH3p4/8/13, the SH3-GL, or the
      endophilin family. These interactions are mediated by SH3 domains and are
      believed to play a regulatory role in synaptic vesicle recycling. We have
      precisely mapped the target peptides on human synaptojanin that are recognized by
      the SH3 domains of endophilins and amphiphysin and proven that they are distinct.
      By a combination of different approaches, selection of phage displayed peptide
      libraries, substitution analyses of peptides synthesized on cellulose membranes, 
      and a peptide scan spanning a 252-residue long synaptojanin fragment, we have
      concluded that amphiphysin binds to two sites, PIRPSR and PTIPPR, whereas
      endophilin has a distinct preferred binding site, PKRPPPPR. The comparison of the
      results obtained by phage display and substitution analysis permitted the
      identification of proline and arginine at positions 4 and 6 in the PIRPSR and
      PTIPPR target sequence as the major determinants of the recognition specificity
      mediated by the SH3 domain of amphiphysin 1. More complex is the structural
      rationalization of the preferred endophilin ligands where SH3 binding cannot be
      easily interpreted in the framework of the "classical" type I or type II SH3
      binding models. Our results suggest that the binding repertoire of SH3 domains
      may be more complex than originally predicted.
FAU - Cestra, G
AU  - Cestra G
AD  - Dipartimento di Biologia, Universita di Roma Tor Vergata, Rome 00133, Italy.
FAU - Castagnoli, L
AU  - Castagnoli L
FAU - Dente, L
AU  - Dente L
FAU - Minenkova, O
AU  - Minenkova O
FAU - Petrelli, A
AU  - Petrelli A
FAU - Migone, N
AU  - Migone N
FAU - Hoffmuller, U
AU  - Hoffmuller U
FAU - Schneider-Mergener, J
AU  - Schneider-Mergener J
FAU - Cesareni, G
AU  - Cesareni G
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 Proteins, Signal Transducing)
RN  - 0 (Carrier Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Library)
RN  - 0 (SH3GL2 protein, human)
RN  - 147954-52-7 (amphiphysin)
RN  - 9DLQ4CIU6V (Proline)
RN  - EC 3.1.3.- (synaptojanin)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
SB  - IM
MH  - *Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Binding, Competitive
MH  - Carrier Proteins/*metabolism
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Humans
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*metabolism
MH  - Peptide Library
MH  - Phosphoric Monoester Hydrolases/*metabolism
MH  - Proline/*metabolism
MH  - *src Homology Domains
EDAT- 1999/11/05 00:00
MHDA- 1999/11/05 00:01
CRDT- 1999/11/05 00:00
PHST- 1999/11/05 00:00 [pubmed]
PHST- 1999/11/05 00:01 [medline]
PHST- 1999/11/05 00:00 [entrez]
AID - 10.1074/jbc.274.45.32001 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 5;274(45):32001-7. doi: 10.1074/jbc.274.45.32001.