PMID- 10613908
OWN - NLM
STAT- MEDLINE
DCOM- 20000204
LR  - 20191023
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 147
IP  - 7
DP  - 1999 Dec 27
TI  - An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a
      novel component of clathrin-coated pits and vesicles.
PG  - 1503-18
AB  - The actin cytoskeleton has been implicated in endocytosis, yet few molecules that
      link these systems have been identified. Here, we have cloned and characterized
      mHip1R, a protein that is closely related to huntingtin interacting protein 1
      (Hip1). These two proteins are mammalian homologues of Sla2p, an actin binding
      protein important for actin organization and endocytosis in yeast. Sequence
      alignments and secondary structure predictions verified that mHip1R belongs to
      the Sla2 protein family. Thus, mHip1R contains an NH(2)-terminal domain
      homologous to that implicated in Sla2p's endocytic function, three predicted
      coiled-coils, a leucine zipper, and a talin-like actin-binding domain at the COOH
      terminus. The talin-like domain of mHip1R binds to F-actin in vitro and
      colocalizes with F-actin in vivo, indicating that this activity has been
      conserved from yeast to mammals. mHip1R shows a punctate immunolocalization and
      is enriched at the cell cortex and in the perinuclear region. We concluded that
      the cortical localization represents endocytic compartments, because mHip1R
      colocalizes with clathrin, AP-2, and endocytosed transferrin, and because mHip1R 
      fractionates biochemically with clathrin-coated vesicles. Time-lapse video
      microscopy of mHip1R-green fluorescence protein (GFP) revealed a blinking
      behavior similar to that reported for GFP-clathrin, and an actin-dependent inward
      movement of punctate structures from the cell periphery. These data show that
      mHip1R is a component of clathrin-coated pits and vesicles and suggest that it
      might link the endocytic machinery to the actin cytoskeleton.
FAU - Engqvist-Goldstein, A E
AU  - Engqvist-Goldstein AE
AD  - Department of Molecular and Cell Biology, University of California, Berkeley,
      Berkeley, California 94720-3202, USA.
FAU - Kessels, M M
AU  - Kessels MM
FAU - Chopra, V S
AU  - Chopra VS
FAU - Hayden, M R
AU  - Hayden MR
FAU - Drubin, D G
AU  - Drubin DG
LA  - eng
SI  - GENBANK/AF221713
GR  - DK32094/DK/NIDDK NIH HHS/United States
GR  - GM50399/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Actins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Detergents)
RN  - 0 (Fungal Proteins)
RN  - 0 (HIP1 protein, human)
RN  - 0 (Hip1 protein, mouse)
RN  - 0 (Hip1r protein, mouse)
RN  - 0 (Membrane Proteins)
RN  - 0 (SLA2 protein, S cerevisiae)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Talin)
SB  - IM
MH  - 3T3 Cells
MH  - Actins/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - COS Cells
MH  - Carrier Proteins/biosynthesis/*chemistry/metabolism
MH  - Coated Pits, Cell-Membrane/*metabolism
MH  - Coated Vesicles/*metabolism
MH  - Cytoskeletal Proteins
MH  - Cytoskeleton/metabolism
MH  - *DNA-Binding Proteins
MH  - Detergents
MH  - Dogs
MH  - Endocytosis/physiology
MH  - Fungal Proteins/biosynthesis/metabolism
MH  - Humans
MH  - Huntington Disease/*metabolism
MH  - Membrane Proteins/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Saccharomyces cerevisiae
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Analysis, Protein
MH  - Sequence Homology, Amino Acid
MH  - Talin/metabolism
PMC - PMC2174256
EDAT- 1999/12/30 00:00
MHDA- 1999/12/30 00:01
CRDT- 1999/12/30 00:00
PHST- 1999/12/30 00:00 [pubmed]
PHST- 1999/12/30 00:01 [medline]
PHST- 1999/12/30 00:00 [entrez]
AID - 10.1083/jcb.147.7.1503 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Dec 27;147(7):1503-18. doi: 10.1083/jcb.147.7.1503.