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Vol. 10, Issue 8, 2687-2702, August 1999
and
*Department of Pharmacology, University of Colorado Health Science
Center, Denver, Colorado 80111; and The clathrin assembly lymphoid myeloid leukemia
(CALM) gene encodes a putative homologue of the clathrin
assembly synaptic protein AP180. Hence the biochemical
properties, the subcellular localization, and the role in endocytosis
of a CALM protein were studied. In vitro binding and
coimmunoprecipitation demonstrated that the clathrin heavy chain is the
major binding partner of CALM. The bulk of cellular CALM was associated
with the membrane fractions of the cell and localized to
clathrin-coated areas of the plasma membrane. In the membrane fraction,
CALM was present at near stoichiometric amounts relative to clathrin.
To perform structure-function analysis of CALM, we engineered chimeric
fusion proteins of CALM and its fragments with the green fluorescent protein (GFP). GFP-CALM was targeted to the plasma membrane-coated pits and also found colocalized with clathrin in the Golgi area. High
levels of expression of GFP-CALM or its fragments with
clathrin-binding activity inhibited the endocytosis of transferrin and
epidermal growth factor receptors and altered the steady-state
distribution of the mannose-6-phosphate receptor in the cell. In
addition, GFP-CALM overexpression caused the loss of clathrin
accumulation in the trans-Golgi network area, whereas the localization
of the clathrin adaptor protein complex 1 in the trans-Golgi network remained unaffected. The ability of the GFP-tagged fragments of CALM to
affect clathrin-mediated processes correlated with the targeting of the
fragments to clathrin-coated areas and their clathrin-binding
capacities. Clathrin-CALM interaction seems to be regulated by
multiple contact interfaces. The C-terminal part of CALM binds
clathrin heavy chain, although the full-length protein exhibited
maximal ability for interaction. Altogether, the data suggest that CALM
is an important component of coated pit internalization machinery,
possibly involved in the regulation of clathrin recruitment to the
membrane and/or the formation of the coated pit.
Institute of Human
Genetics, 37073 Goettingen, Germany
Corresponding author. E-mail address:
alexander.sorkin{at}uchsc.edu.
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